CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority under 35 U.S.C. §119(e) to U.S. Provisional Patent Application No. 60/604,912, filed Aug. 27, 2004, the entirety of which is incorporated by reference herein.
REFERENCE TO GOVERNMENT GRANT This invention was made with United States government support awarded by the National Institutes of Health, Grant # HL069064. The United States has certain rights in this invention.
FIELD OF THE INVENTION The invention relates to combinations of neurochemically active agents for treating a nervous system and the methods of treating a nervous system with the combinatorial treatments.
BACKGROUND OF THE INVENTION The nervous system is comprised of two divisions: the central nervous system (CNS) and the peripheral nervous system (PNS). The CNS includes the brain and the spinal cord and controls most functions of the body and mind. The remainder of the nervous system is the PNS. Nerves of the PNS connect the CNS to sensory organs (such as the eyes and ears), other organs of the body, muscles, blood vessels, and glands. The peripheral nerves include the cranial nerves, the spinal nerves, and roots.
The CNS controls all voluntary movement, such as movement of the legs during walking, and all involuntary movement, such as beating of the heart. The spinal cord connects the body and the brain by transmitting information to and from the body and the brain.
The nervous system can be injured in numerous ways, and injuries can be traumatic. For instance, sudden physical assault on a portion of the nervous system results in a traumatic injury. In the case of a traumatic brain injury, the injury can be focal, i.e., confined to a specific area of the brain, or diffuse, i.e., involving more than one area of the brain.
Injuries to the nervous system include contusions, which are bruises of the nervous system, and blood clots. Blood clots can form in or around the nervous system. For example, when bleeding occurs between the skull and the brain, the blood forms a clot. This puts pressure on the brain, which can lead to changes in brain function.
Spinal cord injuries (SCI) are a particular type of injury to the nervous system. As of the year 2000, approximately 450,000 people in the United States have sustained SCI, with more than 10,000 new cases reported in the United States every year. Motor vehicle accidents are the leading cause of SCI (44 percent), followed by acts of violence (24 percent), falls (22 percent), sports injuries (8 percent), and other causes (2 percent). Of the 10,000 new cases of SCI in the United States each year, 51.7% have tetraplegia, i.e., injuries to one of the eight cervical segments of the spinal cord, and 56.7% have paraplegia, i.e., lesions in the thoracic, lumbar, or sacral regions of the spinal cord. Since 1990, the most frequent neurologic category is incomplete tetraplegia (29.5%), followed by complete paraplegia (27.9%), incomplete paraplegia (21.3%), and complete tetraplegia (18.5%).
With spinal cord injuries in the neck, significant impairment of breathing may result. The most frequent site of spinal injury is the neck or cervical region and, of these, the major cause of death arises from respiratory complications. For patients that survive a major spinal cord injury in the neck, they may spend the rest of their lives depending on an artificial ventilator or phrenic nerve pacemaker to sustain their lives. For others with less severe respiratory impairment, they may be able to breathe normally, but are unable to sigh or breathe deeply and maintain the integrity of the lung. As a consequence, regions of the lung will collapse in these patients, causing pneumonia and allowing other respiratory infections to become established. Clearly, restoration of normal breathing ability, including deep breaths and sighs, is a major goal in the treatment of spinal cord injury patients.
Injury to the spinal cord and other parts of the nervous system may be particularly devastating to life and the quality of life. In addition, injury to the nervous system can engender serious economic losses to the individual and to society. Currently, there are few effective treatment options available for patients with spinal cord injuries, although there are a few promising indications that physical therapy or chronic intermittent hypoxia (CIH), may have beneficial effects. Exposure to intermittent hypoxic episodes has been shown to initiate spinal protein synthesis. However, studies have also shown that chronic intermittent hypoxia has other drawbacks as a treatment for spinal cord injuries. For example, certain CIH treatment methods can cause systemic hypertension, altered sympathetic chemoreflexes, and hippocampal cell death by the process of apoptosis.
Physical training and preconditioning have been used to treat SCI. Almost all patients with spinal cord injuries can now achieve a partial return of function with proper physical therapy that maintains flexibility and function of the muscles and joints, and strengthens the neural pathways that underlie movement. Physical therapy can also help reduce the risk of blood clots and boost the patient's morale. Physical training currently being investigated includes body weight-supported treadmill training, in which patients with partial spinal cord injury “walk” on a treadmill while they are partially supported through the use of a specially designed harness attached to an overhead lift. Unfortunately, this type of therapy is very expensive, and efficacy is far from complete.
SUMMARY OF THE INVENTION The invention, which is defined by the claims set out at the end of this disclosure, is intended to solve at least some of the problems noted above. A composition is provided that includes an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The composition also includes an effective amount of a neurotrophin.
In another embodiment, the composition also includes an effective amount of at least one of a growth factor and a neuropeptide.
Also provided is a method of treating an injury to a nervous system of an animal. In one embodiment, the method includes the steps of identifying the injury to the nervous system and applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect.
In another embodiment, an injury to the nervous system is identified. An effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect is combined with an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide. The combination is applied to the injury.
A kit is also provided. In an embodiment, the kit includes at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The kit also includes a neurotrophin. In another embodiment, the kit also includes a viscous substance. In some embodiments, the kit also includes at least one of a growth factor and a neuropeptide.
BRIEF DESCRIPTION OF THE DRAWINGS Preferred exemplary embodiments of the invention are illustrated in the accompanying drawings in which:
FIG. 1 is a graph showing change in body weight at 2 weeks after spinal cord injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, the body weight is shown for spinal injury alone (black bar) and for spinal injury and a trophic factor combination made in accordance with the invention (grey bar). In addition, corresponding data are shown for all rats combined.
FIG. 2 is a graph showing peak neurogram voltages from the phrenic nerve during inspiration on the side of injury (Y-axis) at 2 weeks post-injury in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, neurogram voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.
FIG. 3 is a graph showing evoked potential voltage (in volts) from the phrenic neurogram on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). The stimulating current was 1000 uA. For each strain of rats, evoked potential voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.
FIG. 4 is a graph showing the stimulating current (in uAmps) required to evoke potentials in the phrenic nerve on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, stimulating currents are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.
FIG. 5 is a graph showing the change in body mass in grams at 2 weeks post-injury (Y-axis) in different Lewis rats (X-axis). The body weight is shown for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs). FIG. 5 also shows change in phrenic amplitude at 2 weeks post-injury (Y-axis) in the rats (X-axis) for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs).
Before explaining embodiments of the invention in detail, it is to be understood that the invention is not limited in its application to the details of construction and the arrangement of the components set forth in the following description or illustrated in the drawings. The invention is capable of other embodiments or being practiced or carried out in various ways. Also, it is to be understood that the phraseology and terminology employed herein is for the purpose of description and should not be regarded as limiting.
DETAILED DESCRIPTION Definitions
To facilitate understanding of the invention, a number of terms are defined below.
As used herein, the term “antimicrobial polypeptide” refers to polypeptides that inhibit the growth of microbes (e.g., bacteria). Examples of antimicrobial polypeptides include, but are not limited to, the polypeptides described in Tables 1 and 2 below. Antimicrobial polypeptides include peptides synthesized from both L-amino and D-amino acids.
As used herein, the term “pore forming agent” refers to any agent (e.g., peptide or other organic compound) that forms pores in a biological membrane. When the pore forming agent is a peptide, the peptide can be synthesized from both L-amino and D-amino acids.
As used herein, the term “growth factor” refers to any compound that is involved in cell differentiation and growth. Growth factors can be proteins (e.g., IGF-1 (insulin-like growth factor 1), IGF-2 (insulin-like growth factor 2), NGF-β (nerve growth factor-β), EGF (epidermal growth factor), CSGF (colony-stimulating growth factor), FGF (fibroblast growth factor), PDGF (platelet-derived growth factor), VEGF (vascular endothelial growth factor), TGF-β (transforming growth factor β, and bone morphogenetic proteins)), either purified from natural sources or genetically engineered, as well as fragments, mimetics, and derivatives or modifications thereof. Further examples of growth factors are provided in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.
The term “trophic factor” as used herein refers to a substance that stimulates growth and development or stimulates increased activity.
The term “hyaluronic acid” includes hyaluronic acid and its derivatives, for instance, esters, salts such as the sodium, potassium, magnesium, calcium, alkaline, alkaline earth metals, and the like, and derivatives such as sulphated or polysulphated hyaluronates, or hyaluronates that have been otherwise modified in a manner way such that the function of hyaluronic acid is retained.
The term “recombinant protein” or “recombinant polypeptide” as used herein refers to a protein molecule expressed from a recombinant DNA molecule. In contrast, the term “native protein” or “native polypeptide” is used herein to indicate a protein isolated from a naturally occurring (i.e., a nonrecombinant) source. Molecular biological techniques may be used to produce a recombinant form of a protein or polypeptide with similar or identical properties as compared to the native form of the protein.
Where an amino acid sequence is recited herein to refer to an amino acid sequence of a naturally occurring protein molecule, amino acid sequence and like terms, such as polypeptide or protein are not meant to limit the amino acid sequence to the complete, native amino acid sequence associated with the recited protein molecule.
As used herein in reference to an amino acid sequence or a protein, the term “portion” (as in “a portion of an amino acid sequence”) refers to fragments of that protein. The fragments may range in size from four amino acid residues to the entire amino acid sequence minus one amino acid (e.g., 5, 6, 7, 8, . . . x−1).
As used herein, the term “variant,” when used in reference to a protein, refers to a protein encoded by partially homologous nucleic acids so that the amino acid sequence of the protein varies. As used herein, the term “variant” encompasses proteins encoded by homologous genes having both conservative and nonconservative amino acid substitutions that do not result in a change in protein function, as well as proteins encoded by homologous genes having amino acid substitutions that cause decreased protein function or increased protein function.
As used herein, the term “fusion protein” refers to a chimeric protein containing the protein of interest (e.g., defensins and fragments thereof) joined to a heterologous protein fragment (e.g., the fusion partner which consists of a non-defensin protein). The fusion partner may enhance the solubility of a defensin as expressed in a host cell, may provide an affinity tag to allow purification of the recombinant fusion protein from the host cell or culture supernatant, or both. If desired, the fusion protein may be removed from the protein of interest (e.g., defensin or fragments thereof) by a variety of enzymatic or chemical processes known to the art.
As used herein, the term “purified” refers to molecules, either nucleic or amino acid sequences, that are removed from their natural environment, isolated, or separated. The percent of a purified component is thereby increased in the sample. For example, an isolated defensin is therefore a purified defensin. Substantially purified molecules are at least 60% free, preferably at least 75% free, and more preferably at least 90% free from other components with which they are naturally associated.
The term “gene” as used herein, refers to a DNA sequence that comprises control and coding sequences necessary for the production of a polypeptide or protein precursor. The polypeptide can be encoded by a full length coding sequence or by any portion of the coding sequence, as long as the desired protein activity is retained.
The term “homology” refers to a degree of complementarity. There may be partial homology or complete homology (i.e., identity). A “partially complementary sequence” is one that at least partially inhibits a completely complementary sequence from hybridizing to a target nucleic acid. This situation is referred to using the functional term “substantially homologous.” The inhibition of hybridization of the completely complementary sequence to the target sequence may be examined using a hybridization assay (e.g., Southern or Northern blot, solution hybridization, and the like) under conditions of low stringency. A substantially homologous sequence or probe will compete for and inhibit the binding (i.e., the hybridization) of a completely homologous sequence or probe to a target under conditions of low stringency. This is not to say that conditions of low stringency are such that non-specific binding is permitted; low stringency conditions require that the binding of two sequences to one another be a specific (i.e., selective) interaction. The absence of non-specific binding may be tested by the use of a second target that lacks even a partial degree of complementarity (e.g., less than about 30% identity). In this case, in the absence of non-specific binding, the probe will not hybridize to the second non-complementary target.
When used in reference to a double-stranded nucleic acid sequence such as a cDNA or a genomic clone, the term “substantially homologous” refers to any probe which can hybridize to either or both strands of the double-stranded nucleic acid sequence under conditions of low stringency as described herein.
As used herein, the term “hybridization” is used in reference to the pairing of complementary nucleic acid strands. Hybridization and the strength of hybridization (i.e., the strength of the association between nucleic acid strands) is impacted by many factors well known in the art including the degree of complementarity between the nucleic acids, stringency of the conditions involved affected by such conditions as the concentration of salts, the Tm (melting temperature) of the formed hybrid, the presence of other components (e.g., the presence or absence of polyethylene glycol), the molarity of the hybridizing strands, and the G:C content of the nucleic acid strands.
As used herein, the term “stringency” is used in reference to the conditions of temperature, ionic strength, and the presence of other compounds, under which nucleic acid hybridizations are conducted. With high stringency conditions, nucleic acid base pairing will occur only between nucleic acid fragments that have a high frequency of complementary base sequences. Thus, conditions of medium or low stringency are often required when it is desired that nucleic acids that are not completely complementary to one another be hybridized or annealed together. It is well known in the art that numerous equivalent conditions can be employed to comprise medium or low stringency conditions. The choice of hybridization conditions is generally evident to one skilled in the art and is normally guided by the purpose of the hybridization, the type of hybridization (DNA-DNA or DNA-RNA), and the level of desired relatedness between the sequences (e.g., Sambrook et al., 1989, Nucleic Acid Hybridization, A Practical Approach, IRL Press, Washington D.C., 1985, for a general discussion of the state of the art).
The stability of nucleic acid duplexes is known to decrease with an increased number of mismatched bases, and further to be decreased to a greater or lesser degree depending on the relative positions of mismatches in the hybrid duplexes. Thus, the stringency of hybridization can be used to maximize or minimize stability of such duplexes. Hybridization stringency can be altered, for example, by adjusting the temperature of hybridization; adjusting the percentage of helix destabilizing agents, such as formamide, in the hybridization mix; and adjusting the temperature and/or salt concentration of the wash solutions. For filter hybridizations, the final stringency of hybridizations can be determined by the salt concentration and/or temperature used for the post-hybridization washes.
“High stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH2PO4.H2O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5× Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 0.1×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.
“Medium stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH2PO4.H2O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5× Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 1.0×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.
“Low stringency conditions” comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH2PO4.H2O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.1% SDS, 5× Denhardt's reagent [50× Denhardt's contains per 500 ml: 5 g Ficoll (Type 400, Pharamcia), 5 g BSA (Fraction V; Sigma)] and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 5×SSPE, 0.1% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.
As used herein, the term “Tm” is used in reference to the melting temperature, which is the temperature at which 50% of a population of double-stranded nucleic acid molecules becomes dissociated into single strands. The equation for calculating the Tm of nucleic acids is well known in the art. The Tm of a hybrid nucleic acid can be estimated using a formula adopted from hybridization assays in 1 M salt, and commonly used for calculating Tm for PCR primers: [(number of A+T)×2° C.+(number of G+C)×4° C.]. (C. R. Newton et al., PCR, 2nd Ed., Springer-Verlag (New York, 1997), p. 24). This formula was found to be inaccurate for primers longer than 20 nucleotides. (Id.) Another simple estimate of the Tm value can be calculated by the equation: Tm=81.5+0.41(% G+C), when a nucleic acid is in aqueous solution at 1 M NaCl. (e.g., Anderson and Young, Quantitative Filter Hybridization, in Nucleic Acid Hybridization (1985). Other more sophisticated computations exist in the art which take structural as well as sequence characteristics into account for the calculation of Tm. A calculated Tm is merely an estimate; the optimum temperature is commonly determined empirically.
As used herein, the term “vector” is used in reference to nucleic acid molecules that transfer DNA segment(s) from one cell to another and capable of replication in a cell. Vectors may include plasmids, bacteriophages, viruses, cosmids, and the like.
The terms “recombinant vector” and “expression vector” as used herein refer to DNA or RNA sequences containing a desired coding sequence and appropriate DNA or RNA sequences necessary for the expression of the operably linked coding sequence in a particular host organism. Prokaryotic expression vectors include a promoter, a ribosome binding site, an origin of replication for autonomous replication in host cells and can also include other sequences, e.g., an optional operator sequence. A “promoter” is defined as a DNA sequence that directs RNA polymerase to bind to DNA and to initiate RNA synthesis. Eukaryotic expression vectors include a promoter, polyadenylation signal and optionally an enhancer sequence.
As used herein the term “coding region” when used in reference to structural gene refers to the nucleotide sequences which encode the amino acids found in the nascent polypeptide as a result of translation of a mRNA molecule. Typically, the coding region is bounded on the 5′ side by the nucleotide triplet ATG, which encodes the initiator methionine, and on the 3′ side by a stop codon (e.g., TAA, TAG, TGA). In some cases, the coding region is also known to initiate by a nucleotide triplet TTG.
The terms “buffer” or “buffering agents” refer to materials that when added to a solution, cause the solution to resist changes in pH.
The term “monovalent salt” refers to any salt in which the metal (e.g., Na, K, or Li) has a net 1+ charge in solution (i.e., one more proton than electron).
The term “divalent salt” refers to any salt in which a metal (e.g., Mg, Ca, or Sr) has a net 2+ charge in solution.
The term “solution” refers to an aqueous mixture.
The term “buffering solution” refers to a solution containing a buffering reagent.
The present invention relates to neurochemically active agents and combinations thereof. Neurochemically active agents include one or more antimicrobial peptide and/or a substance having an antimicrobial peptide effect. Antimicrobial peptides themselves are known to have trophic effects. As such, an antimicrobial peptide and/or a substance having an antimicrobial peptide effect can be used by itself in the methods of the invention. Neurochemically active agents also include one or more growth factor, neurotrophin, and neuropeptide. Combinations of neurochemically active agents are referred to herein as “trophic factor combinations.”
According to the invention, neurochemically active agents can be used alone or in combination to treat injuries to the nervous system, i.e., the central nervous system and the peripheral nervous system. The one or more neurochemically active agents can be used to treat nervous system injuries, including trauma induced injuries, degenerative induced injuries, age induced injuries, and infection induced injuries. Injuries that can be treated include, but are not limited to, spinal cord injury, including severed spinal cords; peripheral nerve damage, brain injuries, e.g., blood clots, tumors, strokes, and ischemis and perfusion; and Parkinson's disease, Alzheimer disease, muscular dystrophy, amyotrophic lateral sclerosis, multiple sclerosis, Pick's disease, prion diseases, Huntington disease, and related disorders.
When applied to a the nervous system, trophic factor combinations of the invention result in at least one of the following: lower loss in body weight after the injury when compared to controls not receiving the trophic factor combinations, strengthened motor recovery in injured animals treated with the trophic factor combination when compared to animals not treated with the trophic factor combination, larger evoked potentials in nerves when compared to controls not receiving the trophic factor combination, and a lower current required to evoke a response (threshold current) when compared to controls not receiving the trophic factor combination.
It is contemplated that the trophic factor combinations of the present invention used to treat injuries of the nervous system result in reduced inflammation, growth of new cells, increased plasticity, among other beneficial effects.
I. Trophic Factor Combinations
The present invention contemplates the use of trophic factor combinations and their individual components for treatment of injuries to the nervous system. Trophic factor combinations according to the invention can include one or more of the following elements: antimicrobial polypeptides (e.g., defensins), a substance having an effect of an antimicrobial peptide, a growth factor, a neurotrophin, and a neuropeptide. Additional components can also be included and are discussed below.
A. Antimicrobial Peptides
In some embodiments, one or more antimicrobial polypeptides and/or one or more substances having an antimicrobial peptide effect are used as a trophic factor to treat an injury to a nervous system. For additional information on antimicrobial peptides, see, for example, Antimicrobial Peptide Protocols, ed. W. M. Shafer, Humana Press, Totowa, N.J., 1997; and databases including http://aps.unmc.edu/AP/main.php (discussed in Wang Z, Wang G., APD: the Antimicrobial Peptide Database, Nucleic Acids Res. 2004 Jan. 1; 32(Database issue):D590-2), http://sdmc.lit.org.sg/Templar/DB/Antimic/, and http://www.bbcm.units.it/˜zelezetsky/hdpdb.html (database of defense peptides) and Table 1 below.
In some embodiments, the antimicrobial peptide is a compound or peptide selected from the following: bovine defensin peptide (BNP-1, Romeo et al., J. Biol. Chem. 263(15):9573-9575 [1988]), magainin (e.g., magainin I, magainin II, xenopsin, xenopsin precursor fragment, caerulein precursor fragment), magainin I and II analogs (PGLa, magainin A, magainin G, pexiganin, Z-12, pexigainin acetate, D35, MSI-78A, MG0 [K10E, K11E, F12W-magainin 2], MG2+ [K10E, F12W-magainin-2], MG4+ [F12W-magainin 2], MG6+ [f12W, E19Q-magainin 2 amide], MSI-238, reversed magainin II analogs [e.g., 53D, 87-ISM, and A87-ISM], Ala-magainin II amide, magainin II amide), cecropin P1, cecropin A, cecropin B, indolicidin, nisin, ranalexin, lactoferricin B, poly-L-lysine, cecropin A (1-8)-magainin II (1-12), cecropin A (1-8)-melittin (1-12), CA(1-13)-MA(1-13), CA(1-13)-ME(1-13), gramicidin, gramicidin A, gramicidin D, gramicidin S, alamethicin, protegrin, histatin, dermaseptin, lentivirus amphipathic peptide or analog, parasin I, lycotoxin I or II, globomycin, gramicidin S, surfactin, ralinomycin, valinomycin, polymyxin B, PM2 [(+/−) 1-(4-aminobutyl)-6-benzylindane], PM2c [(+/−)-6-benzyl-1-(3-carboxypropyl)indane], PM3 [(+/−) 1-benzyl-6-(4-aminobutyl)indane], tachyplesin, buforin I or II, misgurin, melittin, PR-39, PR-26, 9-phenylnonylamine, (KLAKKLA)n, (KLAKLAK)n, where n=1, 2, or 3, (KALKALK)3, KLGKKLG)n, and KAAKKAA)n, wherein N=1, 2, or 3, paradaxin, Bac 5, Bac 7, ceratoxin, mdelin 1 and 5, bombin-like peptides, PGQ, cathelicidin, HD-5, Oabac5alpha, ChBac5, SMAP-29, Bac7.5, lactoferrin, granulysin, thionin, hevein and knottin-like peptides, MPG1, 1bAMP, snakin, lipid transfer proteins, and plant defensins. Exemplary sequences for the above listed compounds are provided in Table 1. In some embodiments, the antimicrobial peptides or substances having an antimicrobial peptide effect (where they are peptides) are synthesized from L-amino acids, while in other embodiments, the peptides are synthesized from or comprise D-amino acids.
The compounds listed above can be isolated and purified from natural sources as appropriate. The compounds can also be produced recombinantly or synthetically, as described below.
In preferred embodiments, the trophic factor combinations of the present invention comprise one or more antimicrobial polypeptides and/or one or more substance having an antimicrobial peptide effect at a concentration of about 0.01 to about 1000 mg/L. In preferred embodiments, the trophic factor combinations comprise a solution comprising one or more antimicrobial polypeptides at a concentration of about 0.1 to about 5 mg/L.
In some embodiments of the present invention, the antimicrobial polypeptide is a defensin. In preferred embodiments, the trophic factor combinations of the present invention comprise one or more defensins. In further preferred embodiments, the trophic factor combination comprises a solution comprising purified defensins at a concentration of about 0.01 to 1000 mg/L. In particularly preferred embodiments, the trophic factor combinations comprise a solution comprising defensins at a concentration of about 0.1 to 5 mg/L. In still further preferred embodiments, the antimicrobial polypeptide is BNP1 (also known as bactanecin and bovine dodecapeptide). In certain embodiments, the defensin comprises the following consensus sequence:
X1CN1CRN2CN3ERN4CN5GN6CCX2, wherein N and X represent conservatively or nonconservatively substituted amino acids and N1=1, N2=3 or 4, N3=3 or 4, N4=1, 2, or 3, N6=5-9, X1 and X2 may be present, absent, or equal from 1-2.
The present invention is not limited to any particular defensin. Indeed, trophic factor combinations comprising a variety of defensins are contemplated. Representative defensins are provided in Tables 1 and 2 below. In general, defensins are a family of highly cross-linked, structurally homologous antimicrobial peptides that can be found in the azurophil granules of polymorphonuclear leukocytes (PMNs) with homologous peptides being present in macrophages (e.g., Selsted et al., Infect. Immun. 45:150-154 [1984]). Originally described as “Lysosomal Cationic Peptides” in rabbit and guinea pig PMN (Zeya et al., Science 154:1049-1051 [1966]; Zeya et al., J. Exp. Med. 127:927-941 [1968]; Zeya et al., Lab. Invest. 24:229-236 [1971]; Selsted et al., [1984], supra.), this mixture was found to account for most of the microbicidal activity of the crude rabbit PMN extract against various microorganisms (Zeya et al., [1966], supra; Lehrer et al., J. Infect. Dis. 136:96-99 [1977]; Lehrer et al., Infect. Immun. 11:1226-1234 [1975]). Six rabbit neutrophil defensins have been individually purified and are designated NP-1, NP-2, NP-3A, NP-3B, NP-4, and NP-5. Their amino acid sequences were determined, and their broad spectra of activity were demonstrated against a number of bacteria (Selsted et al., Infect. Immun. 45:150-154 [1984]), viruses (Lehrer et al., J. Virol. 54:467 [1985]), and fungi (Selsted et al., Infect. Immun. 49:202-206 [1985]; Segal et al., 151:890-894 [1985]). Defensins have also been shown to possess mitogenic activity (e.g., Murphy et al., J. Cell. Physiol. 155:408-13 [1993]).
Four peptides of the defensin family have been isolated from human PMN's and are designated HNP-1, HNP-2, HNP-3, and HNP-4 (Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]; Wilde et al., J. Biol. Chem. 264:11200-11203 [1989]). The amino acid sequences of HNP-1, HNP-2, and HNP-3 differ from each other only in their amino terminal residues, while each of the human defensins are identical to the six rabbit peptides in 10 or 11 of their 29 to 30 residues. These are the same 10 or 11 residues that are shared by all six rabbit peptides. Human defensin peptides have been shown to share with the rabbit defensins a broad spectrum of antimicrobial activity against bacteria, fungi, and enveloped viruses (Ganz et al., [1985], supra).
Three defensins designated RatNP-1, RatNP-2, and RatNP-4, have been isolated from rat (Eisenhauer et al., Infection and Immunity 57:2021-2027 [1989]). A guinea pig defensin (GPNP) has also been isolated, purified, sequenced and its broad spectrum antimicrobial properties verified (Selsted et al., Infect. Immun. 55:2281-2286 [1987]). Eight of its 31 residues were among those invariant in six rabbit and three human defensin peptides. The sequence of GPNP also included three nonconservative substitutions in positions otherwise invariant in the human and rabbit peptides. Of the defensins tested in a quantitative assay HNP-1, RatNP-1, and rabbit NP-1 possess the most potent antimicrobial properties, while NP-5 possesses the least amount of antimicrobial activity when tested against a panel of organisms in stationary growth phase (Selsted et al., Infect. Immun. 45:150-154 [1984]; Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]). Defensin peptides are further described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777 (each of which is incorporated herein by reference).
Defensin peptides suitable for use alone in the methods and/or in trophic factor combinations of the present invention include natural defensin peptides isolated from known cellular sources, synthetic peptides produced by solid phase or recombinant DNA techniques, and defensin analogs which may be smaller peptides or other molecules having similar binding and biological activity as the natural defensin peptides (e.g., peptide mimetics). Methods for the purification of defensin peptides are described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777, the disclosures of which are incorporated herein by reference.
In preferred embodiments, suitable synthetic peptides will comprise all or part of the amino acid sequence of a known peptide, more preferably incorporating at least some of the conserved regions identified in Table 2. In particularly preferred embodiments, the synthetic peptides incorporate at least one of the conserved regions, more typically incorporating two of the conserved regions, preferably conserving at least three of the conserved regions, and more preferably conserving four or more of the conserved regions. In preferred embodiments, the synthetic peptides comprise fifty amino acids or fewer, although there may be advantages in increasing the size of the peptide above that of the natural peptides in certain instances. In certain embodiments, the peptides have a length in the range from about 10 to 50 amino acids, preferably being in the range from about 10 to 40 amino acids, and most preferably being in the range from about 30 to 35 amino acids which corresponds generally to the length of the natural defensin peptides.
In some cases, it may be desirable to incorporate one or more non-natural amino acids in the synthetic defensin peptides of the present invention. In preferred embodiments, non-natural amino acids comprise at least an N-terminus and a C-terminus of the peptide and have side chains that are either identical to or chemically modified or substituted from a natural amino acid counterpart. An example of a non-natural amino acid is an optical isomer of a naturally-occurring L-amino acid, such as a peptide containing all D-amino acids. Examples of the synthesis of peptides containing all D-amino acids include Merrifield et al., Ciba Found Symp. 186:5-26 (1994); Wade et al., Proc. Natl. Acad. Sci. USA 87(12):4761-5 (1990); and U.S. Pat. No. 5,792,831, which is herein incorporated by reference. Examples of chemical modifications or substitutions include hydroxylation or fluorination of C—H bonds within natural amino acids. Such techniques are used in the manufacture of drug analogs of biological compounds and are known to one of ordinary skill in the art.
Synthetic peptides having biological and binding activity the same or similar to that of natural defensin peptides can be produced by either of two exemplary approaches. First, the polypeptides can be produced by the well-known Merrifield solid-phase chemical synthesis method wherein amino acids are sequentially added to a growing chain (Merrifield, J. Am. Chem. Soc. 85:2149-2156 [1963]). Automatic peptide synthesis equipment is available from several commercial suppliers, including PE Biosystems, Inc., Foster City, Calif.; Beckman Instruments, Inc., Waldwick, N.J.; and Biosearch, Inc., San Raphael, Calif. Using such automatic synthesizers according to manufacturer's instructions, peptides can be produced in gram quantities for use in the present invention.
Second, the synthetic defensin peptides of the present invention can be synthesized by recombinant techniques involving the expression in cultured cells of recombinant DNA molecules encoding a gene for a desired portion of a natural or analog defensin molecule. The gene encoding the defensin peptide can itself be natural or synthetic. Conveniently, polynucleotides can be synthesized by well-known techniques based on the desired amino acid sequence. For example, short single-stranded DNA fragments can be prepared by the phosphoramidite method (Beaucage et al., Tetra. Lett. 22:1859-1862 [1981]). A double-stranded fragment can then be obtained either by synthesizing the complementary strand and annealing the strands together under appropriate conditions, or by adding the complementary strand using DNA polymerase under appropriate conditions, or by adding the complementary strand using DNA polymerase with an appropriate primer sequence. The natural or synthetic DNA fragments coding for the desired defensin peptide can then be incorporated in a suitable DNA construct capable of introduction to and expression in an in vitro cell culture. The DNA fragments can be portions or variants of wild-type nucleic acids encoding defensins. Suitable variants include those both with conservative and nonconservative amino acid substitutions.
The methods, compositions, and trophic factor combinations of the present invention can also employ synthetic non-peptide compositions that have biological activity functionally comparable to that of known defensin peptides. By functionally comparable, it is meant that the shape, size, flexibility, and electronic configuration of the non-peptide molecule is such that the biological activity of the molecule is similar to defensin peptides. In particular, the non-peptide molecules should display comparable mitogenic activity and/or antimicrobial activity or pore forming ability, preferably possessing both activities. Such non-peptide molecules will typically be small molecules having a molecular weight in the range from about 100 to about 1000 daltons. The use of such small molecules is frequently advantageous in the preparation of trophic factor combinations. Candidate mimetics can be screened in large numbers to identify those having the desired activity.
The identification of such nonpeptide analog molecules can be performed using techniques known in the art of drug design. Such techniques include, but are not limited to, self-consistent field (SCF) analysis, configuration interaction (CI) analysis, and normal mode dynamics computer analysis, all of which are well described in the scientific literature (e.g., Rein et al., Computer-Assisted Modeling of Receptor-Ligand Interactions, Alan Liss, N.Y., [1989]). Preparation of the identified compounds will depend on the desired characteristics of the compounds and will involve standard chemical synthetic techniques (e.g., Cary et al., Advanced Organic Chemistry, part B, Plenum Press, New York [1983]).
In some embodiments of the present invention, one or more substances having an effect that an antimicrobial peptide has can be used. Effects that antimicrobial peptides have include, but are not limited to, the following: form pores on the cell membrane; enter cells without membrane lysis and, once in the cytoplasm, bind to, and inhibit the activity of specific molecular targets essential to bacterial growth, thereby causing cell death; induce expression of syndecan, an integral membrane proteoglycan associated largely with epithelial cells, in mesenchymal cells and inhibit the NADPH oxidase activity of neutrophils, suggesting a role of this peptide in wound repair and inflammation; exert a protective effect in various animal models of ischemia-reperfusion injury, preventing the post-ischemic oxidant production; induce angiogenesis both in vitro and in vivo; inhibit membrane protein synthesis; inhibit DNA synthesis; antitumor effect; stimulate cell proliferation; interfere with signal pathways; chemoattractant for immune cells; stimulate cytokine expression; stimulate adhesion molecule expression; angiogenesis; and chloride secretion. TABLE 1
Human Antimicrobial Peptides
Organism
Protein Name Name Length Sequence
Antibacterial 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV
peptide LL-37 LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
precursor PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
EDCDFKKDGLVKRCMGTVNLNQARGSFDIS
CDKDNKRFALLGDFFRKSKEKIGKEFKRIVQR
IKDFLRNLVPRTES
Antibacterial Homo 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV
protein FALL- sapiens LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
39 precursor PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI
KDFLRNLVPRTES
Antimicrobial Homo 476 MQPVMLALWSLLLLWGLATPCQELLETVGTL
peptide RYA3 sapiens ARIDKDELGKAIQNSLVGEPILQNVLGSVTAV
NRGLLGSGGLLGGGGLLGHGGVFGVVEELS
GLKIEELTLPKVLLKLLPGFGVQLSLHTKVGM
HCSGPLGGLLQLAAEVNVTSRVALAVSSRGT
PILILKRCSTLLGHISLFSGLLPTPLFGVVEQM
LFKVLPGLLCPVVDSVLGVVNELLGAVLGLVS
LGALGSVEFSLATLPLISNQYIELDINPIVKSVA
GDIIDFPKSRAPAKVPPKKDHTSQVMVPLYLF
NTTFGLLQTNGALDMDITPELVPSDVPLTTTD
LAALLPEALGKLPLHQQLLLFLRVREAPTVTL
HNKKALVSLPANIHVLFYVPKGTPESLFELNS
VMTVRAQLAPSATKLHISLSLERLSVKVASSF
THAFDGSRLEEWLSHVVGAVYAPKLNVALDV
GIPLPKVLNINFSNSVLEIVENAVVLTVAS
Azurocidin Homo 251 MTRLTVLALLAGLLASSRAGSSPLLDIVGGRK
precursor sapiens ARPRQFPFLASIQNQGRHFCGGALIHARFVM
TAASCFQSQNPGVSTVVLGAYDLRRRERQS
RQTFSISSMSENGYDPQQNLNDLMLLQLDRE
ANLTSSVTILPLPLQNATVEAGTRCQVAGWG
SQRSGGRLSRFPRFVNVTVTPEDQCRPNNV
CTGVLTRRGGICNGDGGTPLVCEGLAHGVA
SFSLGPCGRGPDFFTRVALFRDWIDGVLNNP
GPGPA
Bactericidal Homo 483 MARGPCNAPRWVSLMVLVAIGTAVTAAVNP
permeability- sapiens GVVVRISQKGLDYASQQGTAALQKELKRIKIP
increasing DYSDSFKIKHLGKGHYSFYSMDIREFQLPSS
protein QISMVPNVGLKFSISNANIKISGKWKAQKRFL
precursor (BPI) KMSGNFDLSIEGMSISADLKLGSNPTSGKPTI
(CAP 57) TCSSCSSHINSVHVHISKSKVGWLIQLFHKKIE
SALRNKMNSQVCEKVTNSVSSKLQPYFQTLP
VMTKIDSVAGINYGLVAPPATTAETLDVQMK
GEFYSENHHNPPPFAPPVMEFPAAHDRMVY
LGLSDYFFNTAGLVYQEAGVLKMTLRDDMIP
KESKFRLTTKFFGTFLPEVAKKFPNMKIQIHV
SASTPPHLSVQPTGLTFYPAVDVQAFAVLPN
SSLASLFLIGMHTTGSMEVSAESNRLVGELKL
DRLLLELKHSNIGPFPVELLQDIMNYIVPILVLP
RVNEKLQKGFPLPTPARVQLYNVVLQPHQNF
LLFGADVVYK
bactericidal/per- Homo 487 MRENMARGPCNAPRWVSLMVLVAIGTAVTA
meability- sapiens AVNPGVVVRISQKGLDYASQQGTAALQKELK
increasing RIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQL
protein PSSQISMVPNVGLKFSISNANIKISGKWKAQK
precursor RFLKMSGNFDLSIEGMSISADLKLGSNPTSGK
PTITCSSCSSHINSVHVHISKSKVGWLIQLFHK
KIESALRNKMNSQVCEKVTNSVSSKLQPYFQ
TLPVMTKIDSVAGINYGLVAPPATTAETLDVQ
MKGEFYSENHHNPPPFAPPVMEFPAAHDRM
VYLGLSDYFFNTAGLVYQEAGVLKMTLRDDM
IPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIH
VSASTPPHLSVQPTGLTFYPAVDVQAFAVLP
NSSLASLFLIGMHTTGSMEVSAESNRLVGEL
KLDRLLLELKHSNIGPFPVELLQDIMNYIVPILV
LPRVNEKLQKGFPLPTPARVQLYNVVLQPHQ
NFLLFGADVVYK
beta defensin Homo 111 MKSLLFTLAVFMLLAQLVSGNWYVKKCLNDV
126 sapiens GICKKKCKPEEMHVKNGWAMCGKQRDCCV
preproprotein; PADRRANYPVFCVQTKTTRISTVTATTATTTL
epididymal MMTTASMSSMAPTPVSPTG
secretory
protein
ESP13.2; beta
defensin 26;
chromosome
20 open
reading frame
8
beta-defensin Homo 65 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
sapiens CKNNCGKNEELIALCQKFLKCCRTIQPCGSII
D
Beta-defensin Homo 67 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
103 precursor sapiens RVRGGRCAVLSCLPKEEQIGKCSTRGRKCC
(Beta-defensin RRKK
3) (DEFB-3)
(BD-3) (hBD-3)
(HBD3)
(Defensin like
protein)
Beta-defensin Homo 72 MQRLVLLLAVSLLLYQDLPVRSEFELDRICGY
104 precursor sapiens GTARCRKKCRSQEYRIGRCPNTYACCLRKW
(Beta-defensin DESLLNRTKP
4) (DEFB-4)
(BD-4) (hBD-4)
beta-defensin Homo 77 MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS
105 sapiens QPFPSGEFAVCESCKLGRGKCRKECLENEK
PDGNCRLNFLCCRQR
Beta-defensin Homo 78 MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS
105 precursor sapiens QPFPSGEFAVCESCKLGRGKCRKECLENEK
(Beta-defensin PDGNCRLNFLCCRQRI
5) (DEFB-5)
(BD-5)
beta-defensin Homo 57 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
106 sapiens CKNNCGKNEELIALCQKSLKCCRTI
Beta-defensin Homo 65 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT
106 precursor sapiens CKNNCGKNEELIALCQKSLKCCRTIQPCGSII
(Beta-defensin D
6) (DEFB-6)
(BD-6)
Beta-defensin Homo 63 MKIFVFILAALILLAQIFQARTAIHRALISKRME
107 precursor sapiens GHCEAECLTFEVKIGGCRAELAPFCCKNR
(Beta-defensin
7) (DEFB-7)
(Fragment)
beta-defensin Homo 59 MRIAVLFFTIFFFMSQVLPAKGKFKEICERPN
108 sapiens GSCRDFCLETEIHVGRCLNSRPCCLPL
Beta-defensin Homo 73 MRIAVLLFAIFFFMSQVLPARGKFKEICERPN
108 precursor sapiens GSCRDFCLETEIHVGRCLNSQPCCLPLGHQP
(Beta-defensin RIESTTPKKD
8) (DEFB-8)
Beta-defensin Homo 123 MKLLLLALPMLVLLPQVIPAYSGEKKCWNRS
118 precursor sapiens GHCRKQCKDGEAVKDTCKNLRACCIPSNED
(Beta-defensin HRRVPATSPTPLSDSTPGIIDDILTVRFTTDYF
18) (DEFB-18) EVSSKKDMVEESEAGRGTETSLPNVHHSS
(Epididymal
secretory
protein 13.6)
(ESP13.6)
Beta-defensin Homo 84 MKLLYLFLAILLAIEEPXISGKRHILRCMGNSGI
119 precursor sapiens CRASCKKNEQPYLYCRNCQSCCLQSYMRISI
(Beta-defensin SGKEENTDWSYEKQWPRLP
19) (DEFB-19)
Beta-defensin Homo 88 MKLLYLFLAILLAIEEPVISVECWMDGHCRLLC
120 precursor sapiens KDGEDSIIRCRNRKRCCVPSRYLTIQPVTIHGI
(Beta-defensin LGWTTPQMSTTAPKMKTNITNR
20) (DEFB-20)
Beta-defensin Homo 67 MKLLLLTLTVLLLLSQLTPGGTQRCWNLYGK
123 precursor sapiens CRYRCSKKERVYVYCINNKMCCVKPKYQPK
(Beta-defensin ERWWPF
23) (DEFB-23)
Beta-defensin Homo 43 EFKRCWKGQGACQTYCTRQETYMHLCPDA
124 (Beta- sapiens SLCCLSYALKPPPV
defensin 24)
(DEFB-24)
(Fragment)
Beta-defensin Homo 152 MLTFIICGLLTRVTKGSFEPQKCWKNNVGHC
125 precursor sapiens RRRCLDTERYILLCRNKLSCCISIISHEYTRRP
(Beta-defensin AFPVIHLEDITLDYSDVDSFTGSPVSMLNDLIT
25) (DEFB-25) FDTTKFGETMTPETNTPETTMPPSEATTPET
TMPPSETATSETMPPPSQTALTHN
Beta-defensin Homo 111 MKFLLFTLAVFMLLAQLVSGNWYVKKCLNDV
126 precursor sapiens GICKKKCKPEEMHVKNGWAMCGKQRDCCV
(Beta-defensin PADRRANYPVFCVQTKTTRISTVTATTATTTL
26) (DEFB-26) MMTTASMSSMAPTPVSPTG
(Epididymal
secretory
protein 13.2)
(ESP13.2)
Beta-defensin Homo 99 MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGH
127 precursor sapiens CRKICRVNEVPEALCENGRYCCLNIKELEACK
(Beta-defensin KITKPPRPKPATLALTLQDYVTIIENFPSLKTQ
27) (DEFB-27) ST
Beta-defensin Homo 183 MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG
129 precursor sapiens RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI
(Beta-defensin KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ
29) (DEFB-29) RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS
ATISTMTPGQITYTATSTKSNTKESRDSATAS
PPPAPPPPNILPTPSLELEEAEEQ
Beta-defensin Homo 70 MRVLFFVFGVLSLMFTVPPGRSFISNDECPS
131 precursor sapiens EYYHCRLKCNADEHAIRYCADFSICCKLKIIEI
(Beta-defensin DGQKKW
31) (DEFB-31)
Beta-Defensin Homo 37 PVTCLKSGAICHPVFCPRRYKQIGTCGLPGT
2 sapiens KCCKKP
Beta-defensin Homo 64 MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL
2 precursor sapiens KSGAICHPVFCPRRYKQIGTCGLPGTKCCKK
(BD-2) (hBD-2) P
(Skin-
antimicrobial
peptide 1)
(SAP1)
beta-defensin Homo 156 MNILMLTFIICGLLTRVTKGSFEPQKCWKNNV
25 precursor sapiens GHCRRRCLDTERYILLCRNKLSCCISIISHEYT
RRPAFPVIHLEDITLDYSDVDSFTGSPVSMLN
DLITFDTTKFGETMTPETNTPETTMPPSEATT
PETTMPPSETATSETMPPPSQTALTHN
beta-defensin Homo 93 MKLFLVLIILLFEVLTDGARLKKCFNKVTGYCR
28 precursor sapiens KKCKVGERYEIGCLSGKLCCANDEEEKKHVS
FKKPHQHSGEKLSVLQDYIILPTITIFTV
Beta-Defensin Homo 45 GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGK
3 sapiens CSTRGRKCCRRKK
beta-defensin Homo 95 MKFLLLVLAALGFLTQVIPASAGGSKCVSNTP
32 precursor sapiens GYCRTCCHWGETALFMCNASRKCCISYSFL
PKPDLPQLIGNHWQSRRRNTQRKDKKQQTT
VTS
Beta-defensin- Homo 47 GNFLTGLGHRSDHYNCISSGGQCLYSACPIF
1 (Fragment) sapiens TKIQGTCYRGKAKCCK
Beta-Defensin- Homo 41 GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGL
2 sapiens PGTKCCKKP
Beta-defensin- Homo 67 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
3 sapiens RVRGGRCAVLSRLPKEEQIGKCSTRGRKCC
RRKK
Calgranulin A Homo 93 MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDD
(Migration sapiens LKKLLETECPQYIRKKGADVWFKELDINTDGA
inhibitory VNFQEFLILVIKMGVAAHKKSHEESHKE
factor-related
protein 8)
(MRP-8)
(Cystic fibrosis
antigen)
(CFAG) (P8)
(Leukocyte L1
complex light
chain) (S100
calcium-binding
protein A8)
(Calprotectin
L1L subun
Calgranulin B Homo 114 MTCKMSQLERNIETIINTFHQYSVKLGHPDTL
(Migration sapiens NQGEFKELVRKDLQNFLKKENKNEKVIEHIME
inhibitory DLDTNADKQLSFEEFIMLMARLTWASHEKMH
factor-related EGDEGPGHHHKPGLGEGTP
protein 14)
(MRP-14)
(P14)
(Leukocyte L1
complex heavy
chain) (S100
calcium-
binding protein
A9)
(Calprotectin
L1H subunit)
Calgranulin C Homo 92 MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGE
(CAGC) sapiens LKQLLTKELANTIKNIKDKAVIDEIFQGLDANQ
(CGRP) DEQVDFQEFISLVAIALKAAHYHTHKE
(Neutrophil
S100 protein)
(Calcium-
binding protein
in amniotic fluid
1) (CAAF1)
(p6) [Contains:
Calcitermin]
cathelicidin Homo 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQV
antimicrobial sapiens LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR
peptide PTMDGDPDTPKPVSFTVKETVCPRTTQQSP
EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI
KDFLRNLVPRTES
Cathepsin G Homo 255 MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSR
precursor (EC sapiens PYMAYLQIQSPAGQSRCGGFLVREDFVLTAA
3.4.21.20) (CG) HCWGSNINVTLGAHNIQRRENTQQHITARRAI
RHPQYNQRTIQNDIMLLQLSRRVRRNRNVNP
VALPRAQEGLRPGTLCTVAGWGRVSMRRGT
DTLREVQLRVQRDRQCLRIFGSYDPRRQICV
GDRRERKAAFKGDSGGPLLCNNVAHGIVSY
GKSSGVPPEVFTRVSSFLPWIRTTMRSFKLL
DQMETPL
chromogranin Homo 457 MRSAAVLALLLCAGQVTALPVNSPMNKGDTE
A; parathyroid sapiens VMKCIVEVISDTLSKPSPMPVSQECFETLRGD
secretory ERILSILRHQNLLKELQDLALQGAKERAHQQK
protein 1 KHSGFEDELSEVLENQSSQAELKEAVEEPSS
KDVMEKREDSKEAEKSGEATDGARPQALPE
PMQESKAEGNNQAPGEEEEEEEEATNTHPP
ASLPSQKYPGPQAEGDSEGLSQGLVDREKG
LSAEPGWQAKREEEEEEEEEAEAGEEAVPE
EEGPTVVLNPHPSLGYKEIRKGESRSEALAV
DGAGKPGAEEAQDPEGKGEQEHSQQKEEE
EEMAVVPQGLFRGGKSGELEQEEERLSKEW
EDSKRWSKMDQLAKELTAEKRLEGQEEEED
NRDSSMKLSFRARAYGFRGPGPQLRRGWR
PSSREDSLEAGLPLQVRGYPEEKKEEEGSAN
RRPEDQELESLSAIEAELEKVAHQLQALRRG
Defensin 5 Homo 94 MRTIAILAAILLVALQAQAESLQERADEATTQK
precursor sapiens QSGEDNQDLAISFAGNGLSALRTSGSQARAT
(Defensin, CYCRTGRCATRESLSGVCEISGRLYRLCCR
alpha 5)
Defensin 6 Homo 101 MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK
sapiens AYEADAQEQRGANDQDFAVSFAEDASSSLR
ALGGSTRAFTCHCRRSCYSTEYSYGTCTVM
GINHRFCCL
Defensin 6 Homo 100 MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK
precursor sapiens AYEADAQEQRGANDQDFAVSFAEDASSSLR
(Defensin, ALGSTRAFTCHCRRSCYSTEYSYGTCTVMGI
alpha 6) NHRFCCL
defensin alpha- Homo 65 CCSPGADCSGHPRSGCFPCMGRKLGSKAS
3 precursor sapiens RLKEKHGLLLQNTSVHCRRTSLWNLHLPGKT
(mistranslated) LGILL
defensin beta Homo 60 MKIFFFILAALILLAQIFQARTAIHRALISKRME
107 sapiens GHCEAECLTFEVKIGGCRAELAPFCC
defensin beta Homo 52 GKFKEICERPNGSCRDFCLETEIHVGRCLNS
108 sapiens QPCCLPLGHQPRIESTTPKKD
Defensin beta Homo 21 SCTAIGGRCKNQCDDSEFRIS
112 (Fragment) sapiens
Defensin beta Homo 39 KRYGRCKRDCLESEKQIDICSLPGKICCTEKL
114 (Fragment) sapiens YEEDDMF
defensin beta Homo 101 GEKKCWNRSGXCRKQCKDGEAVKDTCKNX
118 sapiens RACCIPSNEDHRRVPATSPTPLSDSTPGIIDDI
LTVRFTTDYFEVSSKKDMVEESEAGRGTETS
LPNVHHSS
defensin beta Homo 94 SLLFTLAVFMLLAQLVSGNWYVKKCLNDVGI
126 sapiens CKKKCKPEEMHVKNGWAMCGKQRDCCVPA
DRRANYPVFCVQTKTTRISTVTATTATTTLMM
TT
defensin beta Homo 59 EQLKKCWNNYVQRHCRKICRVNEVPEALCE
127 sapiens NGRYCCLNIKELEACKKITKPPSPKQHLH
defensin beta Homo 155 MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG
129 sapiens RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI
KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ
RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS
ATISTMTPGQITYTATSTKSNTKESRDS
defensin beta-1 Homo 36 DHYNCVSSGGQCLYSACPIFTKIQGTCYRGK
sapiens AKCCK
Defensin HNP- Homo 30 DCYCRIPACIAGERRYGTCIYQGRLWAFCC
3 - Chain B sapiens
EP2E Homo 80 MKVFFLFAVLFCLVQTNSGDVPPGIRNTICRM
sapiens QQGICRLFFCHSGEKKRDICSDPWNRCCVS
NTDEEGKEKPEMDGRSGI
gene TAP1 Homo 33 GYDTEVGEAGSQLSGGQRQAVALARALIRKP
protein sapiens CV
Hepcidin Homo 84 MALSSQIWAACLLLLLLLASLTSGSVFPQQTG
precursor sapiens QLAELQPQDRAGARASWMPMFQRRRRRDT
(Liver- HFPICIFCCGCCHRSKCGMCCKT
expressed
antimicrobial
peptide)
(LEAP-1)
(Putative liver
tumor
regressor)
(PLTR)
[Contains:
Hepcidin 25
(Hepc25);
Hepcidin 20
(Hepc20)]
High mobility Homo 215 MGKGDPKKPRGKMSSYAFFVQTCREEHKKK
group protein 1 sapiens HPDASVNFSEFSKKCSERWKTMSAKEKGKF
(HMG-1) EDMAKADKARYEREMKTYIPPKGETKKKFKD
PNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIG
DVAKKLGEMWNNTAADDKQPYEKKAAKLKE
KYEKDIAAYRAKGKPDAAKKGVVKAEKSKKK
KEEEEDEEDEEDEEEEEDEEDEDEEEDDDD
E
liver-expressed Homo 81 MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK
antimicrobial sapiens RRPRRMTPFWRGVSLRPIGASCRDDSECITR
peptide 2 LCRKGQQSPPTMLRSMEY
isoform
Liver- Homo 77 MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK
expressed sapiens RRPRRMTPFWRGVSLRPIGASCRDDSECITR
antimicrobial LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Lysozyme C Homo 148 MKALIVLGLVLLSVTVQGKVFERCELARTLKR
precursor (EC sapiens LGMDGYRGISLANWMCLAKWESGYNTRATN
3.2.1.17) (1,4- YNAGDRSTDYGIFQINSRYWCNDGKTPGAV
beta-N- NACHLSCSALLQDNIADAVACAKRVVRDPQG
acetylmurami- IRAWVAWRNRCQNRDVRQYVQGCGV
dase C)
Neutrophil Homo 94 MRTLAILAAILLVALQAQAEPLQARADEVAAA
defensin 1 sapiens PEQIAADIPEVVVSLAWDESLAPKHPGSRKN
precursor MACYCRIPACIAGERRYGTCIYQGRLWAFCC
(HNP-1) (HP-1)
(HP1)
(Defensin,
alpha 1)
[Contains: HP
1-56;
Neutrophil
defensin 2
(HNP-2) (HP-2)
(HP2)]
Neutrophil Homo 94 MRTLAILAAILLVALQAQAEPLQARADEVAAA
defensin 3 sapiens PEQIAADIPEVVVSLAWDESLAPKHPGSRKN
precursor MDCYCRIPACIAGERRYGTCIYQGRLWAFCC
(HNP-3) (HP-3)
(HP3)
(Defensin,
alpha 3)
[Contains: HP
3-56;
Neutrophil
defensin 2
(HNP-2) (HP-2)
(HP2)]
Neutrophil Homo 97 MRIIALLAAILLVALQVRAGPLQARGDEAPGQ
defensin 4 sapiens EQRGPEDQDISISFAWDKSSALQVSGSTRG
precursor MVCSCRLVFCRRTELRVGNCLIGGVSFTYCC
(HNP-4) (HP-4) TRVD
(Defensin,
alpha 4)
Retrocyclin Homo 56 MPCFSWWPCRLRRSHFRQELMKLQPRSSLE
sapiens QMIRKWLMPLHGMKVPLFRFQTQREA
Ribonuclease 7 Homo 156 MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKG
precursor (EC sapiens MTSSQWFKIQHMQPSPQACNSAMKNINKHT
3.1.27.-) KRCKDLNTFLHEPFSSVAATCQTPKIACKNG
(RNase 7) DKNCHQSHGPVSLTMCKLTSGKYPNCRYKE
(Skin-derived KRQNKSYVVACKPPQKKDSQQFHLVPVHLD
antimicrobial RVL
protein 2)
(SAP-2)
Salivary gland Homo 46 MHDFWVLWVLLEYIYNSACSVLSATSSVSSR
antimicrobial sapiens VLNRSLQVKVVKITN
salvic
Secretogranin I Homo 677 MQPTLLLSLLGAVGLAAVNSMPVDNRNHNE
precursor (SgI) sapiens GMVTRCIIEVLSNALSKSSAPPITPECRQVLKT
(Chromogranin SRKDVKDKETTENENTKFEVRLLRDPADASE
B) (CgB) AHESSSRGEAGAPGEEDIQGPTKADTEKWA
[Contains: EGGGHSRERADEPQWSLYPSDSQVSEEVKT
GAWK peptide; RHSEKSQREDEEEEEGENYQKGERGEDSSE
CCB peptide] EKHLEEPGETQNAFLNERKQASAIKKEELVA
RSETHAAGHSQEKTHSREKSSQESGEEAGS
QENHPQESKGQPRSQEESEEGEEDATSEVD
KRRTRPRHHHGRSRPDRSSQGGSLPSEEKG
HPQEESEESNVSMASLGEKRDHHSTHYRAS
EEEPEYGEEIKGYPGVQAPEDLEWERYRGR
GSEEYRAPRPQSEESWDEEDKRNYPSLELD
KMAHGYGEESEEERGLEPGKGRHHRGRGG
EPRAYFMSDTREEKRFLGEGHHRVQENQMD
KARRHPQGAWKELDRNYLNYGEEGAPGKW
QQQGDLQDTKENREEARFQDKQYSSHHTAE
KRKRLGELFNPYYDPLQWKSSHFERRDNMN
DNFLEGEEENELTLNEKNFFPEYNYDWWEK
KPFSEDVNWGYEKRNLARVPKLDLKRQYDR
VAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQ
EAENEKDRADQTVLTEDEKKELENLAAMDLE
LQKIAEKFSQRG
Similar to Homo 226 AEGKWGLAHGRAEAHVWPGQGGWRLGPP
azurocidin 1 sapiens QGRWTGSSPLLDIVGGRKARPRQFPFLASIQ
(Cationic NQGRHFCGGALIHARFVMTAASCFQSQNPG
antimicrobial VSTVVLGAYDLRRRERQSRQTFSISSMSENG
protein 37) YDPQQNLNDLMLLQLDREANLTSSVTILPLPL
(Fragment) QNATVEAGTRCQVAGWGSQRSGGRLSRFP
RFVNVTVTPEDQCRPNNVCTGVLTRRGGICN
VSAPCGGRRGPERY
Nonhuman Animal
Antimicrobial Peptides
Organism
Protein Name Name Length Sequence
11.5 kDa Carcinus 84 NKDCKYWCKDNLGLNYCCGQPGVTYPPFTK
antibacterial maenas KHLGRCPAVRDTCTGVRTQLPTYCPHDGAC
protein QFRSKCCYDTCLKHHVCKTAEYPY
27 kDa Cyprinus 19 GIGGKPVQTAFVDNDGIYD
antibacterial carpio
protein
(Fragment)
4 kDa defensin Androctonus 37 GFGCPFNQGACHRHCRSIRRRGGYCAGLFK
australis QTCTCYR
4 kDa defensin Leiurus 38 GFGCPLNQGACHRHCRSIRRRGGYCAGFFK
(Antibacterial 4 quinquestriatus QTCTCYRN
kDa peptide)
7.5 kDa Ovis aries 164 METQMASPSLGRCSLWLLLLGLLLPSASAQA
bactinecin LSYREAVLRAVGQLNEKSSEVNLYRLLELDP
(Fragment) PPKDAEDQGARKPVSFRVKETVCPRTSQQP
PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
NCNELQSVRRLRPRRPRLPRPRPRPRPRPR
SLPLPRPQPRRI
Abaecin Bombus 39 FVPYNPPRPGQSKPFPSFPGHGPFNPKIQW
pascuorum PYPLPNPGH
Abaecin Apis mellifera 53 MKVVIFIFALLATICAAFAYVPLPNVPQPGRRP
precursor FPTFPGQGPFNPKIKWPQGY
Acaloleptin A1 Acalolepta 71 SLQPGAPNVNNKDQPWQVSPHISRDDSGNT
luxuriosa RTDINVQRHGENNDFEAGWSKVVRGPNKAK
PTWHIGGTHRW
Achacin Achatina 531 MLLLNSALFILCLVCWLPGTSSSRVLTRREGP
precursor fulica QCSRSVDVAVVGAGPSGTYSAYKLRNKGQT
VELFEYSNRIGGRLFTTHLPNVPDLNLESGG
MRYFKNHHKIFGVLVKELNLSNKEFTEGFGK
PGRTRFFARGKSLTLEEMTSGDVPYNLSTEE
KANQANLAGYYLKKLTGFDGEVLTIPQANKLE
VDDGRKLYQLTVDEALDKVGTPEGKEFLKAF
STGNTEFIEGVSAVNYFLVELGEREEEILTLTD
GMSALPQALADAFLKSSTSHALTLNRKLQSL
SKTDNGLYLLEFLETNTHEGYTEESNITDLVC
ARKVILAIPQSALIHLDWKPLRSETVNEAFNAV
KFIPTSKVFLTFPTAWWLSDAVKNPAFVVKST
SPFNQMYDWKSSNVTGDAAMIASYADTSDT
KFQENLNSKGELIPGSAPGANRVTVALKEELL
SQLSQAYGIERSDIPEPKSGTSQFWSSYPFE
GDWTVWKAGYHCEYTQYIIERPSLIDDVFVV
GSDHVNCIENAWTESAFLSVENVFEKYF
Acyl-CoA- Sus scrofa 87 MSQAEFEKAAEEVKNLKTKPADDEMLFIYSH
binding protein YKQATVGDINTERPGILDLKGKAKWDAWNGL
(ACBP) KGTSKEDAMKAYINKVEELKKKYGI
(Diazepam
binding
inhibitor) (DBI)
(Endozepine)
(EP) [Contains:
DBI(32-86)]
Adenoregulin Phyllomedusa 81 MAFLKKSLFLVLFLGLVSLSICEEEKRENEDE
precursor bicolor EEQEDDEQSEMKRGLWSKIKEVGKEAAKAA
(Dermaseptin AKAAGKAALGAVSEAVGEQ
BII)
(Dermaseptin
B2)
Alpha-defensin Macaca 96 MRTLAILAAILLVALQAQAEPLQARTDEATAA
1 mulatta QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
KNMACYCRIPACLAGERRYGTCFYMGRVWA
FCC
Alpha-defensin Macaca 96 MRTLAILAAILLVALQAQAEPLQARTDEATAA
1A mulatta QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
KNMACYCRIPACLAGERRYGTCFYLGRVWA
FCC
Alpha-defensin Macaca 94 MRTLAILAAILLFALLAQAKSLQETADDAATQE
2 mulatta QPGEDDQDLAVSFEENGLSTLRASGSQARR
TCRCRFGRCFRRESYSGSCNINGRIFSLCCR
Alpha-S2 Bos taurus 222 MKFFIFTCLLAVALAKNTMEHVSSSEESIISQE
casein TYKQEKNMAINPSKENLCSTFCKEVVRNANE
precursor EEYSIGSSSEESAEVATEEVKITVDDKHYQKA
[Contains: LNEINQFYQKFPQYLQYLYQGPIVLNPWDQV
Casocidin-I] KRNAVPITPTLNREQLSTSEENSKKTVDMES
TEVFTKKTKLTEEEKNRLNFLKKISQRYQKFA
LPQYLKTVYQHQKAMKPWIQPKTKVIPYVRY
L
Androctonin Androctonus 25 RSVCRQIKICRRRGGCYYKCTNRPY
australis
Andropin Drosophila 57 MKYFVVLVVLALILAITVGPSDAVFIDILDKME
precursor mauritiana NAIHKAAQAGIGIAKPIEKMILPK
Andropin Drosophila 57 MKYFVVLVVLALILAISVGPSDAVFIDILDKVEN
precursor melanogaster AIHNAAQVGIGFAKPFEKLINPK
Andropin Drosophila 67 MKYFLVLVVLTLILAISVGQSDALFVDIIDNVEN
precursor orena AIHKAAKTGIGMVKPIENIFIPNQQKKSTEASN
Andropin Drosophila 57 MKYFVVLVVLALILAITVDPSDAVFIDILDKMEN
precursor sechellia AIHKAAQAGIGLAKPIENMILPK
Andropin Drosophila 60 MKYFVVLVVALILAIAVGPSDAVFIDILDKME
precursor simulans NAIHKAAQAGIGIAKPIENMILPKLTK
Andropin Drosophila 62 MKYFSVLVVLTLILAIVDQSDAFINLLDKVEDA
precursor teissieri LHTGAQAGFKLIRPVERGATPKKSEKPEK
Andropin Drosophila 60 MKYFSVLVVLTLILAISVGQSNAIFVDVLDNVE
precursor yakuba TALHNAAKAGFKLIKPIEKMIMPSKEK
Anionic Bombina 144 MNFKYIFAVSFLIASAYARSVQNDEQSLSQRD
antimicrobial maxima VLEEESLREIRGIGGKILSGLKTALKGAAKELA
peptide STYLHRKRTAEEHEEMKRLEAVMRDLDSLDY
PEEASERETRGFNQDEIANLFTKKEKRILGPV
LGLVSDTLDDVLGILG
Antibacterial Carcinus 30 XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS
6.5 kDa protein maenas
(Fragment)
Antibacterial Bos taurus 158 METQRASLSLGRWSLWLLLLGLALPSASAQA
peptide BMAP- LSYREAVLRAVDQFNERSSEANLYRLLELDP
27 precursor PPKEDDENPNIPKPVSFRVKETVCPRTSQQP
(Myeloid AEQCDFKENGLVKQCVGTVTLDAVKGKINVT
antibacterial CEELQSVGRFKRFRKKFKKLFKKLSPVIPLLH
peptide 27) LG
Antibacterial Bos taurus 159 METQRASLSLGRWSLWLLLLGLALPSASAQA
peptide BMAP- LSYREAVLRAVDQLNEKSSEANLYRLLELDP
28 precursor PPKEDDENPNIPKPVSFRVKETVCPRTSQQS
(Myeloid PEQCDFKENGLLKECVGTVTLDQVGSNFDIT
antibacterial CAVPQSVGGLRSLGRKILRAWKKYGPIIVPIIR
peptide 28) IG
Antibacterial Bos taurus 165 METQRASFSLGRSSLWLLLLGLVVPSASAQD
peptide BMAP- LSYREAVLRAVDQFNERSSEANLYRLLELDP
34 precursor PPEQDVEHPGARKPVSFTVKETVCPRTTPQP
PEQCDFKENGLVKQCVGTVTRYWIRGDFDIT
CNNIQSAGLFRRLRDSIRRGQQKILEKARRIG
ERIKDIFRG
Antibacterial Bombyx mori 59 MNFTRIIFFLFVVVFATASGKPWNIFKEIERAV
peptide ARTRDAVISAGPAVRTVAAATSVASG
enbocin
precursor
(Moricin)
Antibacterial Sus scrofa 153 METQRASLCLGRWSLWLLLLGLVVPSASAQ
peptide PMAP- ALSYREAVLRAVDRLNEQSSEANLYRLLELD
23 precursor QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
(Myeloid PELCDFKENGRVKQCVGTVTLKEIRGNFDITC
antibacterial NQLQSVRIIDLLWRVRRPQKPKFVTVWVR
peptide 23)
Antibacterial Sus scrofa 166 METQRASLCLGRWSLWLLLLGLVVPSASAQ
peptide PMAP- ALSYREAVLRAVDRLNEQSSEANLYRLLELD
36 precursor QPPKADEDPGTPKPVSFTVKETVCPRPTWR
(Myeloid PPELCDFKENGRVKQCVGTVTLNPSNDPLDI
antibacterial NCDEIQSVGRFRRLRKKTRKRLKKIGKVLKWI
peptide 36) PPIVGSIPLGCG
Antibacterial Sus scrofa 167 METQRASLCLGRWSLWLLLLALVVPSASAQA
peptide PMAP- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
37 precursor PPKADEDPGTPKPVSFTVKETVCPRPTWRP
(Myeloid PELCDFKENGRVKQCVGTVTLDQIKDPLDITC
antibacterial NEIQSVGLLSRLRDFLSDRGRRLGEKIERIGQ
peptide 37) KIKDLSEFFQS
Antibacterial Carcinus 88 GLFPNKDCKYWCKDNLGLNYCCGQPGVTYP
protein 11.5 maenas PFTKKHLGRCPAVRDTCTGVRTQLPTYCPHD
kDa GACQFRSKCCYDTCLKHHVCKTAEYPY
(Fragment)
Antibacterial Sus scrofa 172 METQRASLCLGRWSLWLLLLGLVVPSASAQ
protein PR-39 ALSYREAVLRAVDRLNEQSSEANLYRLLELD
precursor QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
PELCDFKENGRVKQCVGTVTLNPSIHSLDISC
NEIQSVRRRPRPPYLPRPRPPPFFPPRLPPRI
PPGFPPRFPPRFPGKR
antibacterial Sus scrofa 172 METQRASLCLGRWSLWLLLLALVVPSASAQA
protein LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
precursor PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLNPSIHSLDISCN
EIQSVRRRPRPPYLPRPRPPPFFPPRLPPRIP
PGFPPRFPPRFPGKR
antibacterial Cavia 42 GLRKKFRKTRKRIQKLGRKIGKTGRKVXKAW
protein, 11 K porcellus REYGQIPYPCR
Antifungal Galleria 76 MKIAFIVAISLAFLAVTSCIEFEKSTESHDIQKR
peptide mellonella GVTITVKPPFPGCVFYECIANCRSRGYKNGG
gallerimycin YCTINGCQCLR
Antifungal Sarcophaga 85 MVKLFVIVILALIAVAFGQHGHGGQDQHGYG
protein peregrina HGQQAVYGKGHEGHGVNNLGQDGHGQHG
precursor YAHGHSDQHGHGGQHGQHDGYKNRGY
(AFP)
Antimicrobial Xenopus 66 LKCVNLQANGIKMTQECAKEDTKCLTLRSLK
amphipathic laevis KTLKFCASGRTCTTMKIMSLPGEQITCCEGN
helix-forming MCNA
peptide
Antimicrobial Acrocinus 34 CIKNGNGCQPDGSQGNCCSRYCHKEPGWV
peptide ALO1 longimanus AGYCR
Antimicrobial Acrocinus 34 CIANRNGCQPDGSQGNCCSGYCHKEPGWV
peptide ALO2 longimanus AGYCR
Antimicrobial Acrocinus 36 CIKNGNGCQPNGSQGNCCSGYCHKQPGWV
peptide ALO3 longimanus AGYCRRK
Antimicrobial Glossina 208 MQSFKICFFISCLSVVLVKGQFGGTVSSNPN
peptide attacin morsitans GGLDVNARLSKTIGDPNANVVGGVFAAGNTD
AttA GGPATRGAFLAANKDGHGLSLQHSKTDNFG
SSLTSSAHAHLFNDKTHKLDANAFHSRTHLD
NGFKFDRVGGGLRYDHVTGHGASLTASRIP
QLDMNTLGLTGKANLWSSPNRATTLDLTGG
VSKHFGGPFDGQTNKQIGLGLNSRF
Antimicrobial Manduca 67 MKFSRVLFFVFACFAAFTVTAAKPWDFLKEL
peptide sexta EGAGQRIRDAIISAQPAVETIAQATAIFKGQSK
cecropin 6 EED
Antimicrobial Gallus gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF
peptide CHP1 YLCCKRIR
(Chicken
heterophil
peptide 1)
Antimicrobial Gallus gallus 34 GRKSDCFRKNGFCAFLKCPYLTLISGLCSXF
peptide CHP2 HLC
(Chicken
heterophil
peptide 2)
(Fragment)
Antimicrobial Glossina 87 MKFYLVLAFLTLCAVAVTALPAGDETRIDLETL
peptide morsitans EEDLRLVDGAQVTGELKRDKRVTCNIGEWV
defensin DefA CVAHCNSKSKKSGYCSRGVCYCTN
Antimicrobial Glossina 76 PQSPPAQIKDPKIYASGGGSPKDGYNVNVDV
peptide morsitans RKNVWVSQNGRHSIDATGGYSQHLGGPYG
diptericin DipA NSRPDFRGGASYTYRF
(Fragment)
Antimicrobial Equus 46 DVQCGEGHFCHDXQTCCRASQGGXACCPY
peptide eNAP- caballus SQGVCCADQRHCCPVGF
1 (Fragment)
Antimicrobial Equus 46 EVERKHPLGGSRPGRCPTVPPGTFGHCACL
peptide eNAP- caballus CTGDASEPKGQKCCSN
2 (Fragment)
Antimicrobial Manduca 171 AILFAAIVACACAQVSMPPQYAQIYPEYYKYS
peptide sexta KQVRHPRDVTWDKQVGNNGKVFGTLGQND
gloverin QGLFGKGGYQHQFFDDHRGKLTGQGYGSR
(Fragment) VLGPYGDSTNFGGRLDWANKNANAALDVTK
SIGGRTGLTASGSGVWQLGKNTDLSAGGTL
SQTLGHGKPDVGFQGLFQHRW
Antimicrobial Sus scrofa 82 MALSVQIRAACLLLLLLVSLTAGSVLPSQTRQ
peptide LTDLRTQDTAGATAGLTPVAQRLRRDTHFPI
hepcidin CIFCCGCCRKAICGMCCKT
Antimicrobial Lumbricus 76 MSLCISDYLYLTLTFSKYERQKDKRPYSERKN
peptide rubellus QYTGPQFLYPPERIPPQKVIKWNEEGLPIYEI
lumbricin1 PGEGGHAEPAAA
Antimicrobial Mytilus 82 MKAVFVLLVVGLCIMMMDVATAGFGCPNNY
peptide galloprovincialis ACHQHCKSIRGYCGGYCASWFRLRCTCYRC
MGD2b GGRRDDVEDIFDIYDNVAVERF
Antimicrobial Manduca 67 MKLTSLFIFVIVALSLLFSSTDAAPGKIPVKAIK
peptide moricin sexta QAGKVIGKGLRAINIAGTTHDWSFFRPKKKK
H
Antimicrobial Equus 160 MKKMGCGGRLSSCPTMTSRALLLLASALLGT
peptide NK- caballus PGLTFSGLNPESYDLATAHLSDGEQFCQGLT
lysin QEDLQGDLLTERERQGIACWSCRKILQKLED
LVGEQPNEATINEAASRVCRNLGLLRGACKKI
MRTCLRLISRDILAGKKPQEVCVDIKLCKHKA
GLI
Antimicrobial Xenopus 24 GVLSNVIGYLKKLGTGALNAVLKQ
peptide PGQ laevis
Antimicrobial Meleagris 65 MRIVYLLFPFILLLAQGAAGSSLALGKREKCL
peptide THP1 gallopavo RRNGFCAFLKCPTLSVISGTCSRFQVCCKTLL
precursor G
(Turkey
heterophil
peptide 1)
Antimicrobial Meleagris 64 MRILYLLFSLLFLALQVSPGLSSPKRDMLFCK
peptide THP2 gallopavo RGTCHFGRCPSHLIKVGSCFGFRSCCKWPW
precursor DA
(Turkey
heterophil
peptide 2)
Antimicrobial Meleagris 25 LSCKRGTCHFGRCPSHLIKGSCSGG
peptide THP3 gallopavo
(Turkey
heterophil
peptide 3)
(Fragment)
Antimicrobial Manduca 207 KMFTKFVVLVCLLVGAKARPQLGALTFNSDG
protein attacin sexta TSGAAVKVPFGGNKNNIFSAIGGADFNANHK
2 (Fragment) LSSATAGVALDNIRGHGLSLTDTHIPGFGDKL
TAAGKLNLFHNNNHDLTANAFATRNMPNIPQ
VPNFNTVGGGLDYMFKNKVGASLGAAHTDFI
NRNDYSVGGKLNLFRNPSTSLDFNAGFKKFD
TPFMRSGWEPNMGFSLSKFF
Antimicrobial Oryctolagus 171 METHKHGPSLAWWSLLLLLLGLLMPPAIAQD
protein CAP18 cuniculus LTYREAVLRAVDAFNQQSSEANLYRLLSMDP
precursor (18 QQLEDAKPYTPQPVSFTVKETECPRTTWKLP
kDa EQCDFKEDGLVKRCVGTVTRYQAWOSFDIR
lipopolysacchar- CNRAQESPEPTGLRKRLRKFRNKIKEKLKKIG
ide- binding QKIQGFVPKLAPRTDY
protein) (18
kDa cationic
protein)
(CAP18-A)
Antimicrobial- Pheretima 67 MYSKYERQKDKRPYSERKDQYTGPQFLYPP
like peptide tschiliensis DRIPPSKAIKWNEEGLPMYEVLPDGAGAKTA
PP-1 VEAAAE
Apidaecin Bombus 17 GNRPVYIPPPRPPHPRL
pascuorum
apidaecin Ib Apis mellifera 26 EAKPEAKPGNNRPVYIPQPRPPHPRL
precursor
Apidaecin Apis mellifera 168 MKNFALAILVVTFVVAVFGNTNLDPPTRPARL
precursor, type RREAKPEAEPGNNRPIYIPQPRPPHPRLRRE
14 AEPKAEPGNNRPIYIPQPRPPHPRLRREAES
EAEPGNNRPVYIPQPRPPHPRLRREPEAEPG
NNRPVYIPQPRPPHPRLRREPEAEPGNNRPV
YIPQPRPPHPRI
Apidaecin Apis mellifera 144 MKNFALAILVVTFVVAVFGNTNLDPPTRPTRL
precursor, type RREAEPEAEPGNNRPVYIPQPRPPHPRLRRE
22 AEPEAEPGNNRPVYIPQPRPPHPRLRREAEP
EAEPGNNRPVYIPQPRPPHPRLRREAEPEAE
PGNNRPVYIPQPRPPHPRI
Apidaecin Apis mellifera 283 KNFALAILVVTFVVAVFGNTNLDPPTRPTRLR
precursor, type REAKPEAEPGNNRPVYIPQPRPPHPRLRREA
73 (Fragment) EPEAEPGNNRPVYIPQPRPPHPRLRREAELE
AEPGNNRPVYISQPRPPHPRLRREAEPEAEP
GNNRPVYIPQPRPPHPRLRREAELEAEPGNN
RPVYISQPRPPHPRLRREAEPEAEPGNNRPV
YIPQPRPPHPRLRREAEPEAEPGNNRPVYIP
QPRPPHPRLRREAEPEAEPGNNRPVYIPQPR
PPHPRLRREAKPEAKPGNNRPVYIPQPRPPH
PRI
Apolipoprotein Bos taurus 76 QAEESNLQSLVSQYFQTVADYGKDLVEKAK
A-II (Apo-AII) GSELQTQAKAYFEKTQEELTPFFKKAGTDLL
(Antimicrobial NFLSSFIDPKKQPAT
peptide BAMP-
1)
ASABF Ascaris suum 93 MKTAIIVVLLVIFASTNAAVDFSSCARMDVPGL
precursor SKVAQGLCISSCKFQNCGTGHCEKRGGRPT
(ASABF-alpha) CVCDRCGRGGGEWPSVPMPKGRSSRGRR
HS
ASABF-epsilon Ascaris suum 65 MVTKGIVLFMLVILFASTDAATCGYDDAKLNR
(ASABF- PTIGCILSCKVQGCETGACYLRDSRPICVCKR
epsilon2) C
ASABF-zeta Ascaris suum 94 MKAILIALLLTTFTVVNGGVVLTSCARMDTPVL
SKAAQGLCITSCKYQNCGTGFCQKVGGRPT
CMCRRCANGGGSWPVIPLDTLVKLALKRGK
R
ASABF-zeta2 Ascaris suum 35 TSCKYQNCGTGFCQKVGGRPTCMCRRCAN
(Fragment) GGGSWP
Attacin A Drosophila 224 MQKTSILIVALVALFAITEALPSLPTTGPIRVRR
precursor melanogaster QVLGGSLTSNPAGGADARLDLTKGIGNPNHN
VVGQVFAAGNTQSGPVTTGGTLAYNNAGHG
ASLTKTHTPGVKDVFQQEAHANLFNNGRHNL
DAKVFASQNKLANGFEFQRNGAGLDYSHING
HGASLTHSNFPGIGQQLGLDGRANLWSSPN
RATTLDLTGSASKWTSGPFANQKPNFGAGL
GLSHHFG
Attacin A Trichoplusia 254 MFTYKLILGLVLVVSASARYLVFEDLEGESYL
precursor ni VPNQAEDEQVLEGEPFYENAVQLASPRVRR
QAQGSVTLNSDGSMGLGAKVPIVGNEKNVL
SALGSVDLNDQLKPASRGMGLALDNVNGHG
LSVMKETVPGFGDRLTGAGRVNVFHNDNHDI
SAKAFVTKNMPDFPNVPNFNTVGGGVDYMY
KNKVGASLGMANTPFLDRKDYSAMGNLNVF
RSPTTSVDFNAGFKKFDTPVFKSNWEPNFGL
TFSRSFGNKW
Attacin B Drosophila 218 MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG
precursor melanogaster SLASNPAGGADARLNLSKGIGNPNHNVVGQ
VFAAGNTQSGPVTTGGTLAYNNAGHGASLT
KTHTPGVKDVFQQEAHANLFNNGRHNLDAK
VFASQNKLANGFEFQRNGAGLDYSHINGHG
ASLTHSNFPGIGQQLGLDGRANLWSSPNRAT
TLDLTGSASKWTSGPFANQKPNFGAGLGLS
HHFG
Attacin B Hyalophora 233 MFAKLFLVSVLLVGVNSRYVLVEEPGYYDKQ
precursor cecropia YEEQPQQWVNSRVRRQAGALTINSDGTSGA
(Immune VVKVPITGNENHKFSALGSVDLTNQMKLGAA
protein P5) TAGLAYDNVNGHGATLTKTHIPGFGDKMTAA
GKVNLFHNDNHDFSAKAFATKNMPNIPQVPN
FNTVGAGVDYMFKDKIGASANAAHTDFINRN
DYSLGGKLNLFKTPTTSLDFNAGWKKFDTPF
FKSSWEPSTSFSFSKYF
Aftacin E and F Hyalophora 235 MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEH
precursor cecropia YEEPELLASSRVRRDAHGALTLNSDGTSGAV
(Immune VKVPFAGNDKNIVSAIGSVDLTDRQKLGAATA
protein P5) GVALDNINGHGLSLTDTHIPGFGDKMTAAGK
VNVFHNDNHDITAKAFATRNMPDIANVPNFN
TVGGGIDYMFKDKIGASASAAHTDFINRNDYS
LDGKLNLFKTPDTSIDFNAGFKKFDTPFMKSS
WEPNFGFSLSKYF
Attacin Bombyx mori 214 MSKSVALLLLCACLASGRHVPTRARRQAGSF
precursor TVNSDGTSGAALKVPLTGNDKNVLSAIGSAD
(Nuecin) FNDRHKLSAASAGLALDNVNGHGLSLTGTRI
PGFGEQLGVAGKVNLFHNNNHDLSAKAFAIR
NSPSAIPNAPNFNTLGGGVDYMFKQKVGASL
SAAHSDVINRNDYSAGGKLNLFRSPSSSLDF
NAGFKKFDTPFYRSSWEPNVGFSFSKFF
Attacin-A Drosophila 221 MQNTSILIVALVALFAITEALPTTGPIRVRRQVL
CG10146-PA melanogaster GGSLTSNPAGGADARLDLTKGIGNPNHNVV
GQVFAAGNTQSGPVTTGGTLAYNNAGHGAS
LTKTHTPGVKDVFQQEAHANLFNNGRHNLD
AKVFASQNKLANGFEFQRNGAGLDYSHINGH
GASLTHSNFPGIGQQLGLDGRANLWSSPNR
ATTLDLTGSASKWTSGPFANQKPNFGAGLGL
SHHFG
Attacin-B Drosophila 218 MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG
CG18372-PA melanogaster SLASNPAGGADARLNLSKGIGNPNHNVVGQ
VFAAGNTQSGPVTTGGTLAYNNAGHGASLT
KTHTPGVKDVFQQEAHANLFNNGRHNLDAK
VFASQNKLANGFEFQRNGAGLDYSHINGHG
GSLTHSNFPGIGQQLGLDGRANLWSSPNRA
TTLDLTGSASKWTSGPFANQKPNFGAGLGLS
HHFG
Azurocidin Sus scrofa 219 IVGGRRAQPQEFPFLASIQKQGRPFCAGALV
(Cationic HPRFVLTAASCFRGKNSGSASVVLGAYDLRQ
antimicrobial QEQSRQTFSIRSISQNGYDPRQNLNDVLLLQ
protein CAP37) LDREARLTPSVALVPLPPQNATVEAGTNCQV
(Heparin- AGWGTQRLRRLFSRFPRVLNVTVTSNPCLP
binding protein) RDMCIGVFSRRGRISQGDRGTPLVCNGLAQ
(HBP) GVASFLRRRFRRSSGFFTRVALFRNWIDSVL
NNPP
bactenecin 5 Bos taurus 42 RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPP
FRPPLRFP
Bactenecin 5 Ovis aries 176 METQGASLSLGRWSLWLLLLGLVLPSASAQA
precursor LSYREAVLRAVGQLNERSSEANLYRLLELDP
(BAC5) APNDEVDPGTRKPVSFTVKETVCPRTTQQPP
EECDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFRPPFRPPVRPP
IRPPFRPPFRPPIGPFPGRR
Bactenecin 5 Bos taurus 176 METQRASLSLGRCSLWLLLLGLVLPSASAQA
precursor LSYREAVLRAVDQFNERSSEANLYRLLELDP
(BAC5) (PR- TPNDDLDPGTRKPVSFRVKETDCPRTSQQPL
42) EQCDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFYPPFRPPIRPPI
FPPIRPPFRPPLGPFPGRR
Bactenecin 5 Capra hircus 176 METQGASLSLGRWSLWLLLLGLVVPLASAQA
precursor LSYREAVLRAVGQLNERSSEANLYRLLELDP
(CHBAC5) APNDEVDPGTRKPVSFTVKETVCPRTTQQPP
EECDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFNPPFRPPVRPP
FRPPFRPPFRPPIGPFPGRR
bactenecin 7 Bos taurus 59 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPL
PFPRPGPRPIPRPLPFPRPGPRPIPRP
Bactenecin 7 Ovis aries 190 METQMASPSLGRCSLWLLLLGLLLPSASAQA
precursor LSYREAVLRAVGQLNEKSSEVNLYRLLELDP
(BAC7) PPKDAEDQGARKPVSFRVKETVCPRMSQQP
PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
NCNELQSVRRLRPRRPRLPRPRPRPRPRPR
SLPLPRPQPRRIPRPILLPWRPPRPIPRPQPQ
PIPRWL
Bactenecin 7 Bos taurus 190 METQRASLSLGRWSLWLLLLGLVLPSASAQA
precursor LSYREAVLRAVDRINERSSEANLYRLLELDPP
(BAC7) (PR- PKDVEDRGARKPTSFTVKETVCPRTSPQPPE
59) QCDFKENGLVKQCVGTITLDQSDDLFDLNCN
ELQSVRRIRPRPPRLPRPRPRPLPFPRPGPR
PIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPR
PL
beta defensin Mus 74 MKISYFLLLILSLGSSQINPVSGDDSIQCFQKN
39 musculus NTCHTNQCPYFQDEIGTCYDRRGKCCQKRL
LHIRVPRKKKV
Beta defensin 9 Mus 78 MPVTKSYFMTVVVVLILVDETTGGLFGFRSSK
precursor musculus RQEPWIACELYQGLCRNACQKYEIQYLSCPK
(Hypothetical TRKCCLKYPRKITSF
defensin-like
structure
containing
protein)
Beta defensin- Capra hircus 64 MRLHHLLLALFFLVLSAGSGFTQGIINHRSCY
2 precursor RNKGVCAPARCPRNMRQIGTCHGPPVKCCR
KK
Beta-defensin Bos taurus 38 DFASCHTNGGICLPNRCPGHMIQIGICFRPRV
1 (BNDB-1) KCCRSW
(BNBD-1)
Beta-defensin Capra hircus 64 MRLHHLLLVLFFLVLSAGSGFTQGIRSRRSCH
1 precursor RNKGVCALTRCPRNMRQIGTCFGPPVKCCR
(BD-1) KK
Beta-defensin Sus scrofa 64 MRLHRLLLVFLLMVLLPVPGLLKNIGNSVSCL
1 precursor RNKGVCMPGKCAPKMKQIGTCGMPQVKCC
(BD-1) KRK
(Defensin, beta
1)
Beta-defensin Pan 68 MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR
1 precursor troglodytes SDHYNCVSSGGQCLYSACPIFTKIQGTCYRG
(BD-1) (hBD-1) KAKCCK
(Defensin, beta
1)
Beta-defensin Mus 69 MKTHYFLLVMICFLFSQMEPGVGILTSLGRRT
1 precursor musculus DQYKCLQHGGFCLRSSCPSNTKLQGTCKPD
(BD-1) (mBD- KPNCCKS
1)
Beta-defensin Rattus 69 MKTHYFLLVMLFFLFSQMELGAGILTSLGRRT
1 precursor norvegicus DQYRCLQNGGFCLRSSCPSHTKLQGTCKPD
(BD-1) (RBD-1) KPNCCRS
Beta-defensin Macaca 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
1 precursor mulatta SDHYNCVRSGGQCLYSACPIYTRIQGTCYHG
(BD-1) (RhBD- KAKCCK
1) (Defensin,
beta 1)
Beta-defensin Ovis aries 64 MRLHHLLLVLFFVVLSAGSGFTQGVRNRLSC
1 precursor HRNKGVCVPSRCPRHMRQIGTCRGPPVKCC
(BD-1) (sBD1) RKK
Beta-defensin Bos taurus 40 QGVRSYLSCWGNRGICLLNRCPGRMRQIGT
10 (BNDB-10) CLAPRVKCCR
(BNBD-10)
Beta-defensin Bos taurus 38 GPLSCRRNGGVCIPIRCPGPMRQIGTCFGRP
11 (BNDB-11) VKCCRSW
(BNBD-11)
Beta-defensin Macaca 123 MKLLLLALPILVLLPQVIPAYGGEKKCWNRSG
118 precursor mulatta HCRKQCKDGEAVKETCKNHRACCVPSNEDH
(Epididymal RRLPTTSPTPLSDSTPGIIDNILTIRFTTDYFEI
secretory SSKKDMVEESEAGQGTQTSPPNVHHTS
protein 13.6)
(ESP13.6)
Beta-defensin Bos taurus 38 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRP
12 (BNDB-12) VKCCRSW
(BNBD-12)
Beta-defensin Macaca 123 MKSLLFTLAVFMLLAQLVSGNLYVKRCLNDIG
126 precursor fascicularis ICKKTCKPEEVRSEHGWVMCGKRKACCVPA
(Epididymal DKRSAYPSFCVHSKTTKTSTVTARATATTATT
secretory ATAATPLMISNGLISLMTTMAATPVSPTT
protein 13.2)
(ESP13.2)
Beta-defensin Bos taurus 42 SGISGPLSCGRNGGVCIPIRCPVPMRQIGTCF
13 (BNDB-13) GRPVKCCRSW
(BNBD-13)
Beta-defensin Macaca 64 MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL
2 mulatta KNGAICHPVFCPRRYKQIGTCGLPGTKCCKK
P
Beta-defensin Bos taurus 40 VRNHVTCRINRGFCVPIRCPGRTRQIGTCFG
2 (BNDB-2) PRIKCCRSW
(BNBD-2)
Beta-defensin Mus 71 MRTLCSLLLICCLLFSYTTPAVGSLKSIGYEAE
2 precursor musculus LDHCHTNGGYCVRAICPPSARRPGSCFPEK
(BD-2) (mBD- NPCCKYMK
2)
Beta-defensin Rattus 63 MRIHYLLFSFLLVLLSPLSAFTQSINNPITCLTK
2 precursor norvegicus GGVCWGPCTGGFRQIGTCGLPRVRCCKKK
(BD-2) (RBD-2)
Beta-defensin Ovis aries 64 MRLHHLLLVLFFVVLSAGSGFTHGVTDSLSC
2 precursor RWKKGICVLTRCPGTMRQIGTCFGPPVKCC
(BD-2) (sBD2) RLK
Beta-defensin Mus 63 MRIHYLLFAFLLVLLSPPAAFSKKINNPVSCLR
3 precursor musculus KGGRCWNRCIGNTRQIGSCGVPFLKCCKRK
(BD-3) (mBD-
3)
Beta-defensin Bos taurus 57 LALLFLVLSAGSGFTQGVRNHVTCRINRGFC
3 precursor VPIRCPGRTRQIGTCFGPRIKCCRSW
(BNDB-3)
(BNBD-3)
(Fragment)
Beta-defensin Mus 63 MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTN
4 precursor musculus GAICWGPCPTAFRQIGNCGHFKVRCCKIR
(BD-4) (mBD-
4)
Beta-defensin Bos taurus 63 MRLHHLLLAVLFLVLSAGSGFTQRVRNPQSC
4 precursor RWNMGVCIPFLCRVGMRQIGTCFGPRVPCC
(BNDB-4) RR
(BNBD-4)
beta-defensin 4 Mus 63 MRIHYLLFTFLPVLLSPLAAFTQIINNPITCMTN
variant musculus GAICWGPCPTAFRQIGNCGHFKVRCCKIR
Beta-defensin Bos taurus 64 MRLHHLLLVLLFLVLSAGSGFTQVVRNPQSC
5 precursor RWNMGVCIPISCPGNMRQIGTCFGPRVPCC
(BNDB-5) RRW
(BNBD-5)
Beta-defensin Mus 63 MKIHYLLFAFILVMLSPLAAFSQLINSPVTCMS
6 musculus YGGSCQRSCNGGFRLGGHCGHPKIRCCRR
K
Beta-defensin Bos taurus 42 QGVRNHVTCRIYGGFCVPIRCPGRTRQIGTC
6 (BNDB-6) FGRPVKCCRRW
(BNBD-6)
Beta-Defensin Mus 37 NSKRACYREGGECLQRCIGLFHKIGTCNFRF
7 musculus KCCKFQ
Beta-defensin Bos taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC
7 (BNDB-7) LGPRIKCCR
(BNBD-7)
Beta-defensin Mus 71 MRIHYVLFAFLLVLLSPFAAFSQDINSKRACY
7 precursor musculus REGGECLQRCIGLFHKIGTCNFRFKCCKFQIP
EKKTKIL
Beta-Defensin Mus 35 NEPVSCIRNGGICQYRCIGLRHKIGTCGSPFK
8 musculus CCK
Beta-defensin Mus 60 MRIHYLLFTFLLVLLSPLAAFSQKINEPVSCIR
8 (Beta- musculus NGGICQYRCIGLRHKIGTCGSPFKCCK
defensin 6)
Beta-defensin Bos taurus 38 VRNFVTCRINRGFCVPIRCPGHRRQIGTCLG
8 (BNDB-8) PQIKCCR
(BNBD-8)
Beta-defensin Bos taurus 55 LALLFLVLSAGSGFTQGVRNFVTCRINRGFCV
9 precursor PIRCPGHRRQIGTCLAPQIKCCR
(BNDB-9)
(BNBD-9)
(Fragment)
Beta-defensin Bos taurus 53 LALLFLVLSAGSGISGPLSCRRKGGICILIRCP
C7 precursor GPMRQIGTCFGRPVKCCRSW
(BBD(C7))
(Fragment)
Beta-defensin Gallus gallus 80 MRIVYLLIPFFLLFLQGAAGTATQCRIRGGFC
prepropeptide RVGSCRFPHIAIGKCATFISCCGRAYEVDALN
SVRTSPWLLAPGNNPH
Beta-defensin Meleagris 59 MRIVYLLFPFFLLFLQSAAGTPIQCRIRGGFCR
prepropeptide gallopavo FGSCRFPHIAIAKCATFIPCCGSIWG
Beta-defensin- Equus 64 MRILHFLLAFLIVFLLPVPGFTAGIETSFSCSQ
1 caballus NGGFCISPKCLPGSKQIGTCILPGSKCCRKK
Beta-defensin- Mus 85 MKNLPSNMALSREVFYFGFALFFIVVELPSGS
12 musculus WAGLEYSQSFPGGEIAVCETCRLGRGKCRR
(Hypothetical TCIESEKIAGWCKLNFFCCRERI
defensin-like
structure
containing
protein)
Beta-defensin- Pan 64 MRVLYLLFSFLFIELMPLPGVFGGISDPVTCLK
2 troglodytes SGAICHPVFCPRRYKQIGTCGLPGTKCCKKP
beta-defensin-3 Bos taurus 42 QGVRNHVTCRINRGFCVPIRCPGRTRQIGTC
FGPRIKCCRSW
Beta-defensin- Pan 64 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC
3 (Fragment) troglodytes RVRGGRCAVLTCLPKEEQIGKCSTRGRKCC
R
beta-defensin-4 Bos taurus 41 QRVRNPQSCRWNMGVCIPFLCRVGMRQIGT
CFGPRVPCCRR
beta-defensin-5 Bos taurus 40 QVVRNPQSCRWNMGVCIPISCPGNMRQIGT
CFGPRVPCCR
beta-defensin-9 Bos taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC
LGPQIKCCR
Beta-defensin- Canis 65 MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS
like peptide 1 familiaris CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
QR
Beta-defensin- Canis 69 MKAFLLTLAALVLLSQVTSGSAEECWNLRGS
like peptide 2 familiaris CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
QRSVQF
Beta-defensin- Canis 99 MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS
like peptide 3 familiaris CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML
QRNRKDNPKICLELQKILNIQSNLDKEEQSWK
HCTS
Big defensin Tachypleus 79 NPLIPAIYIGATVGPSVWAYLVALVGAAAVTA
tridentatus ANIRRASSDNHSCAGNRGWCRSKCFRHEYV
DTYYSAVCGRYFCCRSR
bombinin H Bombina 20 IIGPVLGMVGSALGGLLKKI
Met-8 variegata
Bombinin Bombina 21 IIGPVLGMVGSALGGLLKKIG
H1/H3 variegata
Bombinin H4 Bombina 21 LIGPVLGLVGSALGGLLKKIG
variegata
Bombinin H5 Bombina 21 IIGPVLGLVGSALGGLLKKIG
variegata
Bombinin-like Bombina 27 GIGSAILSAGKSALKGLAKGLAEHFAN
peptide 2 (BLP- orientalis
2)
Bombinin-like Bombina 25 GIGAAILSAGKSIIKGLANGLAEHF
peptide 4 (BLP- orientalis
4)
Bombinin-like Bombina 144 MNFKYIVAVSFLIASTYARSVKNDEQSLSQRD
peptide 7, BPL- orientalis VLEEESLREIRGIGGALLSAGKSALKGLAKGL
7 precursor AEHFANGKRTAEEHEVMKRLEAVMRDLDSL
DYPEEASEMETRSFNQEEIANLFTKKEKRILG
PVLDLVGRALRGLLKKIG
Bombinin-like Bombina 204 MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 1 orientalis LEEESLREIRGIGASILSAGKSALKGLAKGLAE
precursor HFANGKRTAEDHEVMKRLEAAIQSLSQRDVL
[Contains: EEESLREIRGIGASILSAGKSALKGLAKGLAEH
Acidic peptide FANGKRTAEEHEVMKRLEAVMRDLDSLDYP
1; Bombinin- EEASEMETRSFNQEEIANLYTKKEKRILGPIL
like peptide 1 GLVSNALGGLLG
(BLP-1);
Octapeptide 1;
Acidic peptide
2; Octapeptide
2; Acidic
peptide 3; GH-
1 peptide]
Bombinin-like Bombina 137 MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 1 variegata LEEESLREIRGIGGALLSAAKVGLKGLAKGLA
precursor EHFANGKRTAEEREVMKRLEAAMRDLDSFE
[Contains: HPEEASEKETRGFNQEEKEKRIIGPVLGLVGS
Acidic peptide ALGGLLKKIG
1-1; Bombinin-
like peptide 1
(BLP-1);
Octapeptide 1;
Acidic peptide
1-2; Bombinin
H]
Bombinin-like Bombina 137 MNFKYIVAVSILIASAYARREENNIQSLSQRDV
peptides 2 variegata LEEESLREIRGIGASILSAGKSALKGFAKGLAE
precursor HFANGKRTAEDHEMMKRLEAAVRDLDSLEH
[Contains: PEEASEKETRGFNQEEKEKRIIGPVLGLVGSA
Acidic peptide LGGLLKKIG
2-1; Bombinin-
like peptide 2
(BLP-2);
Octapeptide 2;
Acidic peptide
2-2; Bombinin
H2]
Bombinin-like Bombina 200 MNFKYIVAVSILIASAYARSEENDIQSLSQRDV
peptides 3 orientalis LEEESLREIRGIGAAILSAGKSALKGLAKGLAE
precursor HFGKRTAEDHEVMKRLEAAIHSLSQRDVLEE
[Contains: ESLREIRGIGAAILSAGKSALKGLAKGLAEHF
Acidic peptide GKRTAEEHEMMKRLEAVMRDLDSLDYPEEA
1; Bombinin- SEMETRSFNQEEIANLYTKKEKRILGPILGLVS
like peptide 3 NALGGLLG
(BLP-3);
Octapeptide 1;
Acidic peptide
2; Octapeptide
2; Acidic
peptide 3; GH-
1 peptide]
Bovine Bos taurus 38 APLSCGRNGGVCIPIRCPVPMRQIGTCFGRP
Neutrophil VKCCRSW
Beta-Defensin
12
Brevinin-1 Rana 24 FLPVLAGIAAKVVPALFCKITKKC
brevipoda
Brevinin-1BA Rana 24 FLPFIAGMAAKFLPKIFCAISKKC
berlandieri
Brevinin-1BB Rana 24 FLPAIAGMAAKFLPKIFCAISKKC
berlandieri
Brevinin-1BC Rana 24 FLPFIAGVAAKFLPKIFCAISKKC
berlandieri
Brevinin-1BD Rana 24 FLPAIAGVAAKFLPKIFCAISKKC
berlandieri
Brevinin-1BE Rana 24 FLPAIVGAAAKFLPKIFCVISKKC
berlandieri
Brevinin-1BF Rana 24 FLPFIAGMAANFLPKIFCAISKKC
berlandieri
Brevinin-1E Rana 71 MFTLKKSMLLLFFLGTINLSLCEEERDADEEE
precursor esculenta RRDNPDESEVEVEKRFLPLLAGLAANFLPKIF
CKITRKC
Brevinin-1Ea Rana 24 FLPAIFRMAAKVVPTIICSITKKC
esculenta
brevinin-1Eb Rana 24 VIPFVASVAAEMMQHVYCAASRKC
esculenta
Brevinin-1Eb Rana 23 VIPFVASVAAEMQHVYCAASRKC
esculenta
Brevinin-1LA Rana 24 FLPMLAGLAASMVPKLVCLITKKC
luteiventris
Brevinin-1LB Rana 24 FLPMLAGLAASMVPKFVCLITKKC
luteiventris
Brevinin-1PA Rana pipiens 24 ELPIIAGVAAKVFPKIFCAISKKC
Brevinin-1PB Rana pipiens 24 FLPIIAGIAAKVFPKIFCAISKKC
Brevinin-1PC Rana pipiens 24 FLPIIASVAAKVFSKIFCAISKKC
Brevinin-1PD Rana pipiens 24 FLPIIASVAANVFSKIFCAISKKC
Brevinin-1PE Rana pipiens 24 FLPIIASVAAKVFPKIFCAISKKC
Brevinin-1Sa Rana 24 FLPAIVGAAGQFLPKIFCAISKKC
sphenocephala
Brevinin-1Sb Rana 24 FLPAIVGAAGKFLPKIFCAISKKC
sphenocephala
Brevinin-1Sc Rana 24 FFPIVAGVAGQVLKKIYCTISKKC
sphenocephala
Brevinin-1SY Rana 24 FLPVVAGLAAKVLPSIICAVTKKC
sylvatica
Brevinin-1T Rana 20 VNPIILGVLPKFVCLITKKC
temporaria
Brevinin-1TA Rana 17 FITLLLRKFICSITKKC
temporaria
Brevinin-2 Rana 33 GLLDSLKGFAATAGKGVLQSLLSTASCKLAKT
brevipoda C
Brevinin-2E Rana 33 GIMDTLKNLAKTAGKGALQSLLNKASCKLSG
esculenta QC
Brevinin-2Ea Rana 33 GILDTLKNLAISAAKGAAQGLVNKASCKLSGQ
esculenta C
Brevinin-2Eb Rana 33 GILDTLKNLAKTAGKGALQGLVKMASCKLSG
esculenta QC
Brevinin-2Ec Rana 34 GILLDKLKNFAKTAGKGVLQSLLNTASCKLSG
esculenta QC
Brevinin-2Ed Rana 29 GILDSLKNLAKNAGQILLNKASCKLSGQC
esculenta
Brevinin-2Ee Rana 29 GIFDKLKNFAKGVAQSLLNKASCKLSGQC
esculenta
Brevinin-2Ef Rana 74 MFTMKKSLLLIFFLGTISLSLCQEERNADDDD
precursor esculenta GEMTEEEKRGIMDTLKNLAKTAGKGALQSLV
KMASCKLSGQC
Brevinin-2T Rana 33 GLLSGLKKVGKHVAKNVAVSLMDSLKCKISG
temporaria DC
Brevinin-2Tb Rana 74 MFTMKKSLLLFFFLGTISLSLCQEERNADEDD
precursor temporaria GEMTEEEKRGILDTLKHLAKTAGKGALQSLL
NHASCKLSGQC
Brevinin-2TC Rana 29 GLWETIKNFGKKFTLNILHKLKCKIGGGC
temporaria
Brevinin-2TD Rana 29 GLWETIKNFGKKFTLNILHNLKCKIGGGC
temporaria
buforin I Bufo 129 MSGRGKQGGKVRAKAKTRSSRAGLQFPVG
gargarizans RVHRLLRKGNYAQRVGAGAPVYLAAVLEYLT
AEILELAGNAARDNKKTRIIPRHLQLAVRNDE
ELNKLLGGVTIAQGGVLPNIQAVLLPKTESSK
PAKSK
Buthinin Androctonus 34 SIVPIRCRSNRDCRRFCGFRGGRCTYARQCL
australis CGY
Caeridin Litoria chloris 13 MGLLDGLLGTLGL
1.1/1.2/1.3
Caeridin Litoria 12 GLLDGLLGTLGL
1.1/1.2/1.3 xanthomera
Caeridin 1.4 Litoria chloris 13 MGLLDGLLGGLGL
Caeridin 1.4 Litoria 12 GLLDGLLGGLGL
xanthomera
Caerin 1.1 Litoria 26 MGLLSVLGSVAKHVLPHVVPVIAEHL
caerulea
Caerin 1.1 Litoria 25 GLLSVLGSVAKHVLPHVVPVIAEHL
splendida
Caerin 1.6 Litoria chloris 25 MGLFSVLGAVAKHVLPHVVPVIAEK
Caerin 1.6 Litoria 24 GLFSVLGAVAKHVLPHVVPVIAEK
xanthomera
Caerin 1.7 Litoria chloris 25 MGLFKVLGSVAKHLLPHVAPVIAEK
Caerin 1.7 Litoria 24 GLFKVLGSVAKHLLPHVAPVIAEK
xanthomera
Caerulein Litoria 10 QQDYTGWMDF
xanthomera
cathelin related Mus 172 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS
antimicrobial musculus YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP
peptide QGDEDPDTPKSVRFRVKETVCGKAERQLPE
QCAFKEQGWKQCMGAVTLNPAADSFDISC
NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK
KIGQKIKNFFQKLVPQPE
Cathelin- Mus 173 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS
related musculus YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP
antimicrobial QGDEDPDTPKSVRFRVKETVCGKAERQLPE
peptide QCAFKEQGWKQCMGAVTLNPAADSFDISC
precursor NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK
(Cramp) KIGQKIKNFFQKLVPQPEQ
(Cathelin-like
protein) (CLP)
Cathelin- Ovis aries 160 METQRASLSLGRCSLWLLLLGLALPSASAQV
related peptide LSYREAVLRAADQLNEKSSEANLYRLLELDP
SC5 precursor PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
1 (Antibacterial AEQCDFKENGLLKECVGTVTLDQVRNNFDIT
peptide SMAP- CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
29) (Myeloid RIAG
antibacterial
peptide SMAP-
29)
Cathelin- Ovis aries 160 METQRASLSLGRRSLWLLLLGLVLASASAQA
related peptide LSYREAVLRAVDQLNEKSSEANLYRLLELDP
SC5 precursor PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
2 (Antibacterial AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
peptide SMAP- CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
29) (Myeloid RIAG
antibacterial
peptide SMAP
29)
cathelin-related Ovis aries 160 METQRAGLSLGRRSLWLLLLGLVLASASAQA
protein 1 LSYREAVLRAVDQLNEKSSEANLYRLLELDP
precursor PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
RIAG
cathelin-related Ovis aries 152 SLGRCSLWLLLLGLALPSASAQVLSYREAVL
protein 2 RAADQLNEKSSEANLYRLLELDPPPKQDDEN
precursor SNIPKPVSFRVKETVCPRTSQQPAEQCDFKE
NGLLKECVGTVTLDQVRNNFDITCAEPQSVR
GLRRLGRKIAHGVKKYGPTVLRIIRIAG
Cecropin Bombyx mori 35 RWKIFKKIEKVGQNIRDGIVKAGPAVAVVGQA
(Antibacterial ATI
peptide CM-IV)
Cecropin 1 Ceratitis 63 MNFNKVFILVAIVIAIFAGQTEAGWLKKIGKKIE
precursor capitata RVGQHTRDATIQTIAVAQQAANVAATARG
Cecropin 1 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor virilis ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin 2 Ceratitis 63 MNFNKVLVLLAVIFAVFAGQTEAGWLKKIGKK
precursor capitata IERVGQHTRDATIQTIGVAQQAANVAATLKG
Cecropin 2 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor virilis ERVGQHTRDATIQGLGIAQQAANVAATARG
Cecropin 3 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI
precursor virilis ERIGQHTRDATIQGVGIAQQAANVAATARG
Cecropin A Aedes 59 MNFTKLFLLIAVAVLLLTGQSEAGGLKKLGKK
precursor aegypti LEGAGKRVFNAAEKALPVVAGAKALRK
Cecropin A Bombyx mori 63 MNFVRILSFVFALVLALGAVSAAPEPRWKLFK
precursor KIEKVGRNVRDGLIKAGPAIAVIGQAKSLGK
Cecropin A Trichoplusia 62 MNLVKILFCVFACLVFTVTAVPEPRWKFFKKI
precursor ni EKVGQNIRDGIIKAGPAVAWGQAASITGK
Cecropin A Hyalophora 64 MNFSRIFFFVFACLTALAMVNAAPEPKWKLF
precursor cecropia KKIEKVGQNIRDGIIKAGPAVAWGQATQIAK
(Cecropin C) G
Cecropin A Spodoptera 57 IFFFVFACLLALSAVSAAPEPRWKVFKKIEKV
precursor litura GRNVRDGIIKAGPAIGVLGQAKALG
(Fragment)
Cecropin Drosophila 63 MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIE
A1/A2 melanogaster RVGQHTRDATIQGLGIAQQAANVAATARG
precursor
Cecropin B Antheraea 35 KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAK
pernyi AL
Cecropin B Drosophila 63 MNFNKIFVFVALILAISLGNSEAGWLRKLGKKI
precursor melanogaster ERIGQHTRDASIQVLGIAQQAANVAATARG
Cecropin B Spodoptera 58 ILSFVFACLLALSAVSAAPEPRWKVFKKIEKM
precursor litura GRNIRDGIVKAGPAIEVLGSAKALGK
(Fragment)
Cecropin B Hyalophora 62 MNFSRIFFFVFALVLALSTVSAAPEPKWKVFK
precursor cecropia KIEKMGRNIRNGIVKAGPAIAVLGEAKALG
(Immune
protein P9)
Cecropin B Bombyx mori 63 MNFAKILSFVFALVLALSMTSAAPEPRWKIFK
precursor KIEKMGRNIRDGIVKAGPAIEVLGSAKAIGK
(Lepidopteran
A and B)
Cecropin C Drosophila 63 MNENKIFVFVALILAISLGQSEAGWLKKLGKRI
precursor erecta ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin C Drosophila 63 MNFYKIFVFVALILAISIGQSEAGWLKKLGKRI
precursor mauritiana ERIGQHTRDATIQGLGIAQQAANVAATARG
Cecropin D Bombyx mori 61 MKFSKIFVFVFAIVFATASVSAAPGNFFKDLE
precursor KMGQRVRDAVISAAPAVDTLAKAKALGQG
Cecropin D Hyalophora 62 MNFTKILFFWACVFAMRTVSAAPWNPFKEL
precursor cecropia EKVGQRVRDAVISAGPAVATVAQATALAKGK
Cecropin P1 Sus scrofa 31 SWLSKTAKKLENSAKKRISEGIAIAIQGGPR
ceratotoxin A Ceratitis 29 SIGSALKKALPVAKKIGKIALPIAKAALP
capitata
Ceratotoxin A Ceratitis 71 MANLKAVFLICIVAFIALQCVVAEPAAEDSVVV
precursor 1 capitata KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA
GLVG
Ceratotoxin A Ceratitis 71 MANLKAVFLICIVAFIAFQCVVAEPAAEDSIVV
precursor 2 capitata KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA
GLVG
Ceratotoxin B Ceratitis 29 SIGSAFKKALPVAKKIGKAALPIAKAALP
capitata
Ceratotoxin C Ceratitis 67 MANIKAVFLICIVAFIAFHCVVAEPTAEDSVVV
precursor capitata KRSLGGVISGAKKVAKVAIPIGKAVLPVVAKLV
G
Ceratotoxin D Ceratitis 71 MANLKAVFLICILAFIAFHCWGAPTAEDSIVV
precursor capitata KRSIGTAVKKAVPIAKKVGKVAIPIAKAVLSVV
GQLVG
Chlamysin Chlamys 137 MMYFVLFCLLAAGTTYGSHNFATGIVPHSCL
precursor islandica ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ
AYWEDCGRPGGSLTSCADDIHCSSQCVQHY
MSRYIGHTSCSRTCESYARLHNGGPHGCEH
GSTLGYWGHVQGHGC
Chromogranin Bos taurus 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTE
A precursor VMKCIVEVISDTLSKPSPMPVSKECFETLRGD
(CgA) (Pituitary ERILSILRHQNLLKELQDLALQGAKERTHQQK
secretory KHSSYEDELSEVLEKPNDQAEPKEVTEEVSS
protein I) (SP-I) KDAAEKRDDFKEVEKSDEDSDGDRPQASPG
[Contains: LGPGPKVEEDNQAPGEEEEAPSNAHPLASLP
Vasostatin-1 SPKYPGPQAKEDSEGPSQGPASREKGLSAE
Chromostatin; QGRQTEREEEEEKWEEAEAREKAVPEEESP
Chromacin; PTAAFKPPPSLGNKETQRAAPGWPEDGAGK
Pancreastatin; MGAEEAKPPEGKGEWAHSRQEEEEMARAP
WE-14; QVLFRGGKSGEPEQEEQLSKEWEDAKRWS
Catestatin] KMDQLAKELTAEKRLEGEEEEEEDPDRSMR
LSFRARGYGFRGPGLQLRRGWRPNSREDSV
EAGLPLQVRGYPEEKKEEEGSANRRPEDQE
LESLSAIEAELEKVAHQLEELRRG
chromogranin Bos taurus 170 MPVDIRNHNEEVVTHLRDPADTSEAPGLSAG
B EPPGSQVAKEAKTRYSKSEGQNREEEMVKY
QKRERGEVGSEERLSEGPQRNQTPAKKSSQ
EGNPPLEEESHVGTGALEEGAERLPGELRNY
LDYGEEKGEESAEFPDFYDSEEQMSPQHTA
EDLELQKIAEKFSGTRRG
Chrysophsin-1 Pagrus major 25 FFGWLIKGAIHAGKAIHGLIHRRRH
Chrysophsin-2 Pagrus major 25 FFGWLIRGAIHAGKAIHGLIHRRRH
Chrysophsin-3 Pagrus major 20 FIGLLISAGKAIHDLIRRRH
Cicadin Cicada 55 NEYHGFVDKANNENKRKKQQGRDDFWKPN
(Fragment) flammata NFANRRRKDDYNENYYDDVDAADVV
Citropin 1.1 Litoria citropa 16 GLFDVIKKVASVIGGL
[Contains:
Citropin 1.1.1;
Citropin 1.1.2]
Citropin 1.1.3 Litoria citropa 18 GLFDVIKKVASVIGLASP
Citropin 1.1.4 Litoria citropa 18 GLFDVIKKVASVIGLASQ
Citropin 1.2 Litoria citropa 16 GLFDIIKKVASVVGGL
[Contains:
Citropin 1.2.1;
Citropin 1.2.2;
Citropin 1.2.3]
Citropin 1.2.4 Litoria citropa 18 GLFDIIKKVASVVGLASP
Citropin 1.2.5 Litoria citropa 18 GLFDIIKKVASVVGLASQ
Citropin 1.3 Litoria citropa 16 GLFDIIKKVASVIGGL
Citropin 2.1.3 Litoria citropa 26 GLIGSIGKALGGLLVDVLKPKLQAAS
[Contains:
Citropin 2.1.2;
Citropin 2.1.1;
Citropin 2.1]
Citropin 3.1.2 Litoria citropa 24 DLFQVIKEKLKELTGGVIEGIQGV
[Contains:
Citropin 3.1.1;
Citropin 3.1]
Clavanin A Styela clava 80 MKTTILILLILGLGINAKSLEERKSEEEKVFQFL
precursor GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG
HYAEDNGKHWYDTGDQ
Clavanin B Styela clava 23 VFQFLGRIIHHVGNFVHGFSHVF
Clavanin C Styela clava 80 MKTTILILLILGLGINAKSLEERKSEEEKVFHLL
precursor GKIIHHVGNFVYGFSHVFGDDQQDNGKFYG
HYAEDNGKHWYDTGDQ
Clavanin D Styela clava 80 MKTTILILLILGLGINAKSLEERKSEEEKAFKLL
precursor GRIIHHVGNFVYGFSHVFGDDQQDNGKFYG
HYAEDNGKHWYDTGDQ
Clavanin E Styela clava 80 MKTTILILLILGLGINAKSLEERKSEEEKLFKLL
precursor GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG
YYAEDNGKHWYDTGDQ
Coleoptericin Zophobas 74 SLQGGAPNFPQPSQQNGGWQVSPDLGRDD
atratus KGNTRGQIEIQNKGKDHDFNAGWGKVIRGP
NKAKPTWHVGGTYRR
Corticostatin I Oryctolagus 93 MRTLILLAAILLAALQAQAELFSVNVDEVLDQ
precursor (CS- cuniculus QQPGSDQDLVIHLTGEESSALQVPDTKGICA
I) (Neutrophil CRRRFCPNSERFSGYCRVNGARYVRCCSRR
antibiotic
peptide NP-3A)
(Microbicidal
peptide NP-3A)
(Antiadrenocort-
icotropin
peptide I)
Corticostatin II Oryctolagus 34 GRCVCRKQLLCSYRERRIGDCKIRGVRFPFC
(CS-II) cuniculus CPR
(Neutrophil
antibiotic
peptide NP-3B)
(Microbicidal
peptide NP-3B)
(Antiadrenocort-
icotropin
peptide II)
Corticostatin III Oryctolagus 95 MRTLALLAAILLVALQAQAEHVSVSIDEVVDQ
precursor (CS- cuniculus QPPQAEDQDVAIYVKEHESSALEALGVKAGV
III) VCACRRALCLPRERRAGFCRIRGRIHPLCCR
(Macrophage R
antibiotic
peptide MCP-
1) (NP-1)
(Antiadrenocort-
icotropin
peptide III)
Corticostatin IV Oryctolagus 95 MRTLALLAAILLVALQAQAEHISVSIDEVVDQQ
precursor (CS- cuniculus PPQAEDQDVAIYVKEHESSALEALGVKAGVV
IV) CACRRALCLPLERRAGFCRIRGRIHPLCCRR
(Macrophage
antibiotic
peptide MCP-
2) (NP-2)
(Antiadrenocort-
icotropin
peptide IV)
Corticostatin VI Oryctolagus 34 GICACRRRFCLNFEQFSGYCRVNGARYVRC
(CS-VI) cuniculus CSRR
(Neutrophil
antibiotic
peptide NP-6)
Corticostatin- Oryctolagus 32 MPCSCKKYCDPWEVIDGSCGLFNSKYICCRE
related peptide cuniculus K
RK-1
Crabrolin Vespa crabro 13 FLPLILRKIVTAL
cryptdin Mus 23 CKRRERMNGTCRKGHLLYTLCCR
musculus
cryptdin 12 Mus 35 LRDLVCYCRARGCKGRERMNGTCRKGHLLY
musculus MLCCR
Cryptdin-1 Mus 35 LRDLVCYCRTRGCKRRERMNXTCRKGHLMY
(CR1) musculus TLCCX
Cryptdin-1 Mus 93 MKKLVLLFALVLLGFQVQADSIQNTDEETKTE
precursor musculus EQPGEEDQAVSVSFGDPEGTSLQEESLRDL
(DEFCR) VCYCRSRGCKGRERMNGTCRKGHLLYTLCC
R
cryptdin-10 Mus 35 LRDLVCYCRKRGCKGRERMNGTCRKGHLLY
musculus TLCCR
Cryptdin-10 Mus 92 KTLVLLSALVLLAFQVQADPIQNTDEETKTEE
precursor musculus QPGEDDQAVSVSFGDPEGSSLQEESLRDLV
(Fragment) CYCRKRGCKGRERMNGTCRKGHLLYTMCC
R
cryptdin-11 Mus 35 LRDLVCYCRSRGCKGRERMNGTCRKGHLLY
musculus MLCCR
Cryptdin-11 Mus 85 ALVLLAFQVQADPIQNTDEETKTEEQPGEED
precursor musculus QAVSVSFGDPEGTSLQEESLRDLVCYCRSR
(Fragment) GCKGRERMNGTCRKGHLLYMLCCR
cryptdin-13 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRRGHLM
musculus YTLCCR
Cryptdin-13 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor musculus EQPGEEDQAVSVSFGDPEGTSLQEESLRDL
VCYCRKRGCKRREHMNGTCRRGHLMYTLC
CR
Cryptdin-14 Mus 85 ALVLLAFQVQADPIQNTDEETKTEEQPGEDD
precursor musculus QAVSVSFGDPEGSSLQEESLRDLVCYCRTR
(Fragment) GCKRRERMNGTCRKGHLMHTLCCR
cryptdin-15 Mus 35 LRDLVCYCRKRGCKRREHINGTCRKGHLLY
musculus MLCCR
Cryptdin-15 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor musculus EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRREHINGTCRKGHLLYMLCC
R
cryptdin-16 Mus 35 LRDLVCYCRSRGCKGRERMNGTCRKGHLM
musculus YTLCCR
Cryptdin-16 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor musculus QPGEEDQAVSVSFGDPEGTSLQEESLRDLV
CYCRSRGCKGRERMNGTCRKGHLMYTLCC
R
Cryptdin-17 Mus 82 LLAFQVQADPIQNTDEETKTEEQPGEEDQAV
precursor musculus SVSFGDPEGTSLQEESLRDLVCYCRKRGCK
(CRYP17) RREHMNGTCRKGHLLYTLCCR
(Fragment)
Cryptdin-2 Mus 35 LRDLVCYCRARGXKGRERMNGTXRKGHLLY
(CR2) musculus MXXXX
Cryptdin-2 Mus 93 MKPLVLLSALVLLSFQVQADPIQNTDEETKTE
precursor musculus EQSGEEDQAVSVSFGDREGASLQEESLRDL
VCYCRTRGCKRRERMNGTCRKGHLMYTLC
CR
Cryptdin-3 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor musculus EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRRERMNGTCRKGHLMYTLC
CR
cryptdin-4 Mus 34 LRGLLCYCRKGHCKRGERVRGTCGIRFLYCC
musculus PRR
Cryptdin-4 Mus 92 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor musculus EQPGEEDQAVSISFGGQEGSALHEKSLRGLL
CYCRKGHCKRGERVRGTCGIRFLYCCPRR
Cryptdin-5 Mus 93 MKTFVLLSALVLLAFQVQADPIHKTDEETNTE
precursor musculus EQPGEEDQAVSISFGGQEGSALHEELSKKLI
CYCRIRGCKRRERVFGTCRNLFLTFVFCCS
Cryptdin-6/12 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor musculus QPGEEDQAVSVSFGDPEGTSLQEESLRDLV
CYCRARGCKGRERMNGTCRKGHLLYMLCC
R
cryptdin-7 Mus 35 LRDLVCYCRTRGCKRREHMNGTCRKGHLMY
musculus TLCCR
Cryptdin-7 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEE
precursor musculus QPGEDDQAVSVSFGDPEGSSLQEESLRDLV
CYCRTRGCKRREHMNGTCRKGHLMYTLCC
R
cryptdin-8 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRKGHLM
musculus YTLCCR
Cryptdin-8 Mus 81 LAFQVQADPIQNTDEETKTEEQPGEDDQAVS
precursor musculus VSFGDPEGSSLQEESLRDLVCYCRKRGCKR
(Fragment) REHMNGTCRKGHLMYTLCCR
cryptdin-9 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRKGHLLY
musculus MLCCR
Cryptdin-9 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE
precursor musculus EQPGEEDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRREHMNGTCRKGHLLYMLC
CR
Cryptdin- Mus 116 MKTLVLLSALVLPCFQVQADPIQNTDEETKTE
related protein musculus EQPEEEDQAVSVSFGGTEGSALQDVAQRRF
1C precursor PWCRKCRVCQKCQVCQKCPVCPTCPQCPK
(CRS1C) QPLCEERQNKTAITTQAPNTQHKGC
Cryptdin- Mus 91 MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related protein musculus EQPGEKDQAVSVSFGDPQGSALQDAALGW
4C-1 precursor GRRCPQCPRCPSCPSCPRCPRCPRCKCNP
(CRS4C) K
Cryptdin- Mus 91 MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related protein musculus EQQGEEDQAVSVSFGDPQGSGLQDAALGW
4C-2 precursor GRRCPRCPPCPRCSWCPRCPTCPRCNCNP
(CRS4C) K
Cryptdin- Mus 91 MKKLVLLSAFVLLAFQVQADSIQNTDEETKTE
related protein musculus EQPGEENQAMSVSFGDPEGSALQDAAVGM
4C-4 precursor ARPCPPCPSCPSCPWCPMCPRCPSCKCNP
(CRS4C) K
Cryptdin- Mus 91 MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE
related protein musculus EQPGEENQAVSISFGDPEGYALQDAAIRRAR
4C-5 precursor RCPPCPSCLSCPWCPRCLRCPMCKCNPK
(CRS4C)
Cyclic Bos taurus 155 METPRASLSLGRWSLWLLLLGLALPSASAQA
dodecapeptide LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP
precursor PQDDEDPDSPKRVSFRVKETVCSRTTQQPP
(Bactenecin 1) EQCDFKENGLLKRCEGTVTLDQVRGNFDITC
NNHQSIRITKQPWAPPQAARLCRIVVIRVCR
Cyclic Ovis aries 155 METQRASLSLGRCSLWLLLLGLALPSASAQV
dodecapeptide LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP
precursor PQDDEDPDSPKRVSFRVKETVCPRTTQQPP
(Bactenecin 1) EQCDFKENGLLKRCEGTVTLDQVRGNFDITC
NNHQSIRITKQPWAPPQAARICRIIFLRVCR
DEFB1-like Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein aethiops SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG
KAKCCK
DEFB1-like Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein erythrogaster SDHYICVRSGGQCLYSACPIYTKIQGTCYHG
KAKCCK
DEFB1-like Gorilla gorilla 68 MRTSYLLLFTLCLLLSEIASGGNFLTGLGHRS
protein DHYNCVSSGGQCLYSACPIFTKIQGTCYGGK
AKCCK
DEFB1-like Hylobates 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR
protein concolor SDHYNCVRSGGQCLYSACPIYTKIQGTCYQG
KAKCCK
DEEBI-like Pan 68 MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR
protein troglodytes SDHYNCVSSGGQCLYSACPIFTKIQGTCYGG
KAKCCK
DEFB1-like Presbytis 68 MRTSYLLLFTLCLLMSEMASGDNFLTGLGHR
protein obscura SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG
KAKCCK
DEFB1-like Saguinus 68 MRTSYLLLFILCLVLCDMDSGDTFLTGLGHRS
protein oedipus DHYNCVKGGGQCLYSACPIYTKVQGTCYGG
KAKCCK
DEFB36 Mus 43 MKLLLLTLAALLLVSQLTPGDAQKCWNLHGK
(Fragment) musculus CRHRCSRKESVY
Defensin Aeshna 38 GFGCPLDQMQCHRHCQTITGRSGGYCSGPL
cyanea KLTCTCYR
Defensin Allomyrina 43 VTCDLLSFEAKGFAANHSLCAAHCLAIGRRG
dichotoma GSCERGVCICRR
Defensin Anopheles 102 MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA
gambiae LSGGANLNTLLDELPEETHHAALENYRAKRA
TCDLASGFGVGNNLCAAHCIARRYRGGYCN
SKAVCVCRN
defensin Anopheles 131 NSRVNGATPAKLKLVLLCLPRASSSPQLIMKC
gambiae ATIVCTIAWLAATLLNGSVQAAPQEEAALSG
GANLNTLLDELPEETHHAALENYRAKRATCD
LASGFGVGSSLCAAHCIARRYRGGYCNSKAV
CVCRN
Defensin Bombus 51 VTCDLLSIKGVAEHSACAANCLSMGKAGGRC
pascuorum ENGICLCRKTTFKELWDKRF
Defensin Branchiostoma 117 MEKKTAYCLLFLVLLVPYTALGAVLKRAPAKK
beicheri EKRAVPLAVPLVYWGASVSPAVWNWLLVTF
GAAAVAAAAVTVSDNDSHSCANNRGWCRS
RCFSHEYIDSWHSDVCGSYDCCRPRY
Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
melanogaster HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
melanogaster HVLVHEDANQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVLVAIAFALLTCMAQAQPVSDVDPIPED
melanogaster HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVPVAIAFALLACVAQAQPVSDVDPIPED
melanogaster HVLVHDDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
simulans HALVHEDAHQEWQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Mamestra 98 MLCLADIRIVASCSAAIKSGYGQQPWLAHVA
brassicae GPYANSLFDDVPADSYHAAVEYLRLIPASCYL
LDGYAAGRDDGRAHCIAPRNRRLYCASYQV
CVCRY
Defensin Musca 92 MKYFTMFAFFFVAVCYISQSSASPAPKEEAN
domestica FVHGADALKQLEPELHGRYKRATCDLLSGTG
VGHSACAAHCLLRGNRGGYCNGKGVCVCR
N
Defensin Ornithodoros 73 MNKLFIVALVLALAVATMAHEVHDDIEEPSVP
moubata RVRRGFGCPFNQYECHAHCSGVPGYKGGY
CKGLFKQTCNCY
Defensin Ornithodoros 73 MNKLFIVALVLALAVATMAHEVYDDVEEPSVP
moubata RVRRGYGCPFNQYQCHSHCSGIRGYKGGY
CKGLFKQTCNCY
Defensin Palomena 43 ATCDALSFSSKWLTVNHSACAIHCLTKGYKG
prasina GRCVNTICNCRN
Defensin Phlebotomus 40 ATCDLLSAFGVGHAACAAHCIGHGYRGGYC
duboscqi NSKAVCTCRR
Defensin Pyrocoelia 55 MKLSVFVLVAVMLVLLCCAMQTEARRRCRS
rufa CVPFCGSNERMISTCFSGGVVCCPR
Defensin Pyrrhocoris 43 ATCDILSFQSQWVTPNHAGCALHCVIKGYKG
apterus GQCKITVCHCRR
Defensin Aedes 57 DELPEETYQAAVENYRRKRATCDLLSGFGVG
(Fragment) albopictus DSACAAHCIARRNRGGYCNAKTVCVC
Defensin Apis mellifera 57 FEPLEHFENEERADRHRRVTCDLLSFKGQVN
(Fragment) DSACAANCHSLGKAGGHCEKGVCICR
Defensin 1 Stomoxys 39 ATCDLLSGMGVNHSACAAHCVLRGNRGGYC
(Fragment) calcitrans NSKAVCVCR
Defensin 1 Acalolepta 83 MKFFITFTFVLSLWLTVYSAPREFAEPEEQD
precursor luxuriosa EGHFRVKRFTCDVLSVEAKGVKLNHAACGIH
CLFRRRTGGYCNKKRVCICR
Defensin 1 Stomoxys 79 MKFLNVVAIALLVVACLAVYSNAAPHEGVKEV
precursor calcitrans AAAKPMGITCDLLSLWKVGHAACAAHCLVLG
DVGGYCTKEGLCVCKE
Defensin 1A Stomoxys 79 MKFLNVVAIALLVVACLSVYSNAAPHEGVKEV
precursor calcitrans AAAKPMGITCDLLSLWKVGHAACAAHCLVLG
NVGGYCTKEGLCVCKE
Defensin 2 Stomoxys 97 MKFFSLFPVIVVVVACLTMRANAAPSAGNEV
precursor calcitrans DHHPDYVDGVEALRQLEPELHGRYKRATCD
LLSMWNVNHSACAAHCLLLGKSGGRCNDDA
VCVCRK
Defensin 2A Stomoxys 97 MKFFSLFPVILVVVACLTMRANAAPSAGDEV
precursor calcitrans DHHPDYVDGVEALRQLEPELHGRYKRATCD
LLSMWNVNHSACAAHCLLLGKSGGRCNDDA
VCVCRK
Defensin 5 Rattus 93 MKKLVLLSALVLLALQVEAEPTPKTDEGTKTD
precursor (RD- norvegicus EQPGKEDQWSVSIEGQGDPAFQDAVLRDL
5) (Enteric KCFCRRKSCNWGEGIMGICKKRYGSPILCCR
defensin
Defensin A Aedes 98 MQSLTVICFLALCTGAITSAYPQEPVLADEAR
aegypti PFANSLFDELPEETYQAAVENFRLKRATCDLL
SGFGVGDSACAAHCIARGNRGGYCNSKKVC
VCRN
Defensin A Mytilus edulis 37 GFGCPNDYPCHRHCKSIPGRXGGYCGGXHR
LRCTCYR
Defensin A Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHNDVEEQSV
moubata PRVRRGYGCPFNQYQCHSHCSGIRGYKGGY
CKGTFKQTCKCY
Defensin A Rhodnius 94 MKCILSLVTLFLVAVLVHSHPAEWNTHQQLD
prolixus DALWEPAGEVTEEHVARLKRATCDLFSFRSK
WVTPNHAACAAHCLLRGNRGGRCKGTICHC
RK
defensin A Aedes 37 MKSLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 2; aegypti PFANS
AaDefA2
defensin A Aedes 37 MQSLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 3; aegypti PFANS
AaDefA3
defensin A Aedes 37 MQPLTVICFLALCTGAITSAYPQEPVLADEAR
isoform 4; aegypti PFANS
AaDefA4
Defensin A Aedes 98 MKSITVICFLALCTVAITSAYPQEPVLADEARP
precursor aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
(AADEF) GFGVGDSACAAHCIARGNRGGYCNSKKVCV
CRN
defensin A Aedes 98 MQSITVICFLALCTGAITSAYPQEPVLADEARP
protein isoform aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
5 GFGVGDSACAAHCIARGNRGGYCNSKKVCV
CRN
defensin alpha- Macaca 30 ACYCRIPACLAGERRYGTCFYLGRVWAFCC
1 mulatta
defensin alpha- Macaca 30 ACYCRIPACLAGERRYGTCFYRRRVWAFCC
3 mulatta
defensin alpha- Macaca 33 RRTCRCRFGRCFRRESYSGSCNINGRIFSLC
4 mulatta CR
defensin alpha- Macaca 32 RTCRCRFGRCFRRESYSGSCNINGRIFSLCC
5 mulatta R
defensin alpha- Macaca 33 RRTCRCRFGRCFRRESYSGSCNINGRISSLC
6 mulatta CR
defensin alpha- Macaca 32 RTCRCRFGRCFRRESYSGSCNINGRISSLCC
7 mulatta R
Defensin B Aedes 40 ATCDLLSGFGVGDSACAAHCIARGNRGGYC
aegypti NSQKVCVCRN
Defensin B Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHDDVEEQSV
moubata PRVRRGYGCPFNQYQCHSHCRGIRGYKGG
YCTGRFKQTCKCY
Defensin B Rhodnius 94 MKCILSLVTLFLVAVLVHSHPAEWNTQQELD
prolixus DALWEPAGEVTEEHVARLKRATCDLLSFSSK
WVTPNHAGCAAHCLLRGNRGGHCKGTICHC
RK
Defensin B Mytilus edulis 35 GFGCPNDYPCHRHCKSIPGRYGGYCGGXHR
(Fragment) LRCTC
defensin beta Mus 67 MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFC
14; beta musculus RIRGGRCAVLNCLGKEEQIGRCSNSGRKCC
defensin 14 RKKK
defensin beta Mus 81 MKTFLFLFAVLFFWSQPRMHFFFFDEKCSRI
34; beta musculus NGRCTASCLKNEELVALCWKNLKCCVTVQS
defensin 34 CGRSKGNQSDEGSGHMGTRG
defensin beta Mus 62 MKFSYFLLLLLSLSNFQNNPVAMLDTIACIENK
37; beta musculus DTCRLKNCPRLHNVVGTCYEGKGKCCHKN
defensin 37
defensin beta Mus 63 MKISCFLLLILSLYFFQINQAIGPDTKKCVQRK
38; beta musculus NACHYFECPWLYYSVGTCYKGKGKCCQKRY
defensin 38
defensin beta Mus 73 MKISCFLLMIFFLSCFQINPVAVLDTIKCLQGN
40; beta musculus NNCHIQKCPWFLLQVSTCYKGKGRCCQKRR
defensin 40 WFARNHVYHV
Defensin beta Mus 64 MRIHYLLFAFLLVLLCPLASDFSKTINNPVSCC
5 musculus MIGGICRYLCKGNILQNGNCGVTSLNCCKRK
Defensin C Rhodnius 94 MKCILSLFTLFLVATLVYSYPAEWNSQHQLDD
prolixus AQWEPAGELTEEHLSRMKRATCDLLSLTSK
WFTPNHAGCAAHCIFLGNRGGRCVGTVCHC
RK
defensin C Zophobas 43 FTCDVLGFEIAGTKLNSAACGAHCLALGRTG
atratus GYCNSKSVCVCR
Defensin C Aedes 99 MRTLIWCFVALCLSAIFTTGSALPGELADDV
precursor aegypti RPYANSLFDELPEESYQAAVENFRLKRATCD
LLSGFGVGDSACAAHCIARRNRGGYCNAKK
VCVCRN
Defensin D Aedes 96 VPTVICFLAMCLVAITGAYPQEPVLADEAQSV
precursor albopictus ANSLFDELPEESYQAAVENLRLKRATCDLLS
(AALDEFD) GFGVGDSACAAHCIARGNRGGYCNSKKVCV
(Fragment) CPI
Defensin Heliothis 44 DKLIGSCVWGAVNYTSDCNGECKRRGYKGG
heliomicin virescens HCGSFANVNCWCET
Defensin Heliothis 44 DKLIGSCVWGAVNYTSDCNGECLLRGYKGG
Heliomicin virescens HCGSFANVNCWCET
defensin Aedes 98 MKSITVICFLALCTGSITSAYPQDPVLADEARP
isoform A1 aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
GFGVGDSACAAHCIARGNRGGYCNSKKVCV
CRN
defensin Aedes 98 MKSITVICFLALCTVAITSAYPQEPVLADEARP
isoform B1 aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
GFGVGDSACAAHCIARGNRGGYCNSQKVCV
CRN
defensin Aedes 98 MKSITVICFLALCTGSITSAYPQEPVLADEARP
isoform B2 aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
GFGVGDSACAAHCIARGNRGGYCNSQKVCV
CRN
defensin Aedes 99 MRTLIVVCFVALCLSAIFTTGSALPEELADDVR
isoform C1 aegypti SYANSLFDELPEESYQAAVENFRLKRATCDL
LSGFGVGDSACAAHCIARRNRGGYCNAKKV
CVCRN
Defensin Mgd- Mytilus 39 GFGCPNNYQCHRHCKSIPGRCGGYCGGWH
1 galloprovincialis RLRCTCYRCG
Defensin MGD- Mytilus 38 GFGCPNNYQCHRHCKSIPGRCGGYCGGXH
1 galloprovincialis RLRCTCYRC
Defensin MGD- Mytilus 81 MKAAFVLLWGLCIMTDVATAGFGCPNNYAC
2 precursor galloprovincialis HQHCKSIRGYCGGYCAGWFRLRCTCYRCG
GRRDDVEDIFDIYDNVAVERF
defensin NP-1 Rattus 32 VTCYCRRTRCGFRERLSGACGYRGRIYRLC
norvegicus CR
defensin NP-4 Rattus 31 ACYCRIGACVSGERLTGACGLNGRIYRLCCR
norvegicus
Defensin Anopheles 102 MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA
precursor gambiae LSGGANLNTLLDELPEETHHAALENYRAKRA
TCDLASGFGVGSSLCAAHCIARRYRGGYCN
SKAVCVCRN
Defensin Drosophila 92 MKFFVLVAIAFALLACVAQAQPVSDVDPIPED
precursor melanogaster HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Oryctes 79 MSRFIVFAFIVAMCIAHSLAAPAPEALEASVIR
precursor rhinoceros QKRLTCDLLSFEAKGFAANHSLCAAHCLAIG
RKGGACQNGVCVCRR
defensin Spodoptera 102 MGVKVINVFLLIAVSACLIHAVAGKPNPRDSS
precursor frugiperda VVEEQSLGPIHNEDLEVKVKPETTTTPEPRIP
GRVSCDFEEANEDAVCQEHCLPKGYTYGICV
SHTCSCI
Defensin Culex pipiens 40 ATCDLLSGFGVNDSACAAHCILRGNRGGYC
precursor NGKKVCVCRN
(Fragment)
defensin R-2 Rattus 31 VTCSCRTSSCRFGERLSGACRLNGRIYRLCC
norvegicus
defensin R-5 Rattus 32 VTCYCRSTRCGFRERLSGACGYRGRIYRLC
norvegicus CR
defensin Mus 92 MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE
related musculus EQPGEENQAVSISFGDPEGYALQDAAAIRRA
cryptdin, RRCPPCPSCLSCPWCPRCLRCPMCKCNPK
related
sequence 12
defensin Mus 92 MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related musculus EQQGEEDQAVSVSFGDPQGSGLQDAAALG
cryptdin, WGRRCPRCPPCPRCSWCPRCPTCPRCNCN
related PK
sequence 7
Defensin Mus 60 MRIHYLLFTFLLVLLSPLAAFSQKINDPVTYIR
related peptide musculus NGGICQYRCIGLRHKIGTCGSPFKCCK
Defensin, Zophobas 43 FTCDVLGFEIAGTKLNSAACGAHCLALGRRG
isoforms B and atratus GYCNSKSVCVCR
C
defensin-3 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAA
mulatta QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
KNMACYCRIPACLAGERRYGTCFYRRRVWA
FCC
defensin-8 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAA
mulatta QEQIPTDNPEVWSLAWDESLAPKDSVPGLR
KNMACYCRIPACLAGERRYGTCFYLRRVWA
FCC
defensin-like Mus 5 ICSPK
gene 1C-1 musculus
Defensin-like Ornithorhynchus 42 FVQHRPRDCESINGVCRHKDTVNCREIFLAD
peptide 1 anatinus CYNDGQKCCRK
(DLP-1)
Defensin-like Ornithorhynchus 42 IMFFEMQACWSHSGVCRDKSERNCKPMAW
peptide 2/4 anatinus TYCENRNQKCCEY
(DLP-2/DLP-4)
Defensin-like Ornithorhynchus 38 FEMQYCWSHSGVCRDKSERNNKPMAWTYC
peptide 3 anatinus ENRQKKCEF
(DLP-3)
Defensin-like Mesobuthus 61 MTYAILIIVSLLPISDGISNVVDKYCSENPLDCN
protein TXKS2 martensii EHCLKTKNQIGICHGANGNEKCSCMES
Demidefensin 2 Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA
mulatta AQQQPGADDQGMAHSFTWPENAALPLSESA
KGLRCICTRGFCRLL
Demidefensin 3 Macaca 76 MRTLALHTAMLLLVALHAQAEARQARADEAA
mulatta AQQQPGADDQGMAHSFTWPENAALPLSESE
RGLRCICVLGICRLL
Dermaseptin 1 Phyllomedusa 34 ALWKTMLKKLGTMALHAGKAALGAAADTISQ
(DS I) sauvagei GTQ
Dermaseptin BI Phyllomedusa 78 MDILKKSLFLVLFLGLVSLSICEEEKRENEDEE
precursor bicolor KQDDEQSEMKRAMWKDVLKKIGTVALHAGK
(Dermaseptin AALGAVADTISQGEQ
B1)
Dermaseptin Phyllomedusa 77 MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDE
DRG3 bicolor EEQEDDEQSEEKRALWKTIIKGAGKMIGSLA
precursor KNLLGSQAQPESEQ
(Dermaseptin
3)
Dermatoxin Phyllomedusa 77 MAFLKKSLFLVLFLGLVPLSLCESEKREGENE
precursor bicolor EEQEDDQSEEKRSLGSFLKGVGTTLASVGKV
VSDQFGKLLQAGQG
Diptericin A Protophormia 82 DEKPKLILPTPAPPNLPQLVGGGGGNRKDGF
terraenovae GVSVDAHQKVWTSDNGGHSIGVSPGYSQHL
PGPYGNSRPDYRIGAGYSYNF
diptericin B Protophormia 41 DEKPKLVLPSXAPPNLPQLVGGGGGNNKXG
terraenovae XXVSINAAQKV
diptericin C Protophormia 39 DEKPKLIXPXXAPXNLXQLVGGGGGNNKKXX
terraenovae GVXVXXAQ
Diptericin D Protophormia 101 MKLFYLLVICALSLAVMADEKPKLILPTPAPPN
precursor terraenovae LPQLVGGGGGNRKDGFGVSVDAHQKVWTS
DNGRHSIGVTPGYSQHLGGPYGNSRPDYRI
GAGYSYNFG
Dolabellanin Dolabella 33 SHQDCYEALHKCMASHSKPFSCSMKFHMCL
B2 auricularia QQQ
Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
melanogaster SHPRPIRVRREALAIEDHLTQAAIRPPPILPA
Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
melanogaster SHPRPIRVRREALAIEDHLTQAAIRPPPILPV
Drosocin Drosophila 64 MKFTIVFLLLACVFAMGVATPGKPRPYSPRPT
CG10816-PA melanogaster SHPRPIRVRREALAIEDHLTQAAIRPPPILPA
Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT
precursor melanogaster SHPRPIRVRREALAIEDHLAQAAIRPPPILPA
Drosomycin Drosophila 44 DCLSGRYKGPCAVWDNETCRRVCKEEGRS
melanogaster SGHCSPSLKCWCEGC
Drosomycin Drosophila 70 MMQIKYLFALFAVLMLVVLGANEADADCLSG
precursor melanogaster RYKGPCAVWDNETCRRVCKEEGRSSGHCS
(Cysteine-rich PSLKCWCEGC
peptide)
enbocin Bombyx mori 59 MNFTRIIFFLGVVVFATASGKPWNIFKEIERAV
ARTRDAVISAGPAVATVAAATSVASG
Enhancer of Sus scrofa 32 RADTQTYQPYNKDWIKEKIYVLLRRQAQQAG
rudimentary K
homolog
[Contains:
Antibacterial
peptide 3910]
(Fragment)
entenic beta Bubalus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNPQSC
defensin bubalis HRNKGICVPIRCPGNMRQIGTCLGPPVKCCR
preproprotein RK
Enteric beta- Bos taurus 64 MRLHHLLLTLLFLVLSAGSGFTQGISNPLSCR
defensin LNRGICVPIRCPGNLRQIGTCFTPSVKCCRW
precursor R
Eosinophil Cavia 233 MKLLLLLALLLGAVSTRHLKVDTSSLQSLRGE
granule major porcellus ESLAQDGETAEGATREATAGALMPLPEEEE
basic protein 1 MEGASGSEDDPEEEEEEEEEVEFSSELDVS
precursor PEDIQCPKEEDTVKFFSRPGYKTRGYVMVGS
(MBP-1) ARTFNEAQWVCQRCYRGNLASIHSFAFNYQ
VQCTSAGLNVAQVWIGGQLRGKGRCRRFV
WVDRTVWNFAYWARGQPWGGRQRGRCVT
LCARGGHWRRSHCGKRRPFVCTY
EP2e (ANTI- Mus 69 MKVLLLFAVFFCFVQGNSGDIPPGIRNTVCLM
microbial-like musculus QQGHCRLFMCRSGERKGDICSDPWNRCCV
protein BIN-1B PYSVKDRR
homolog)
Esculentin-1 Rana 46 GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVR
esculenta TGIDIAGCKIKGEC
Esculentin-1A Rana 46 GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVR
esculenta TGIDIAGCKIKGEC
Esculentin-1B Rana 84 MFTLKKPLLLIVLLGMISLSLCEQERNADEEE
precursor esculenta GSEIKRGIFSKLAGKKLKNLLISGLKNVGKEV
GMDVVRTGIDIAGCKIKGEC
Esculentin-2A Rana 37 GILSLVKGVAKLAGKGLAKEGGKFGLELIACKI
esculenta AKQC
Esculentin-2B Rana 37 GLFSILRGAAKFASKGLGKDLTKLGVDLVACK
berlandieri ISKQC
Esculentin-2B Rana 37 GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKI
esculenta AKQC
Esculentin-2L Rana 37 GILSLFTGGIKALGKTLFKMAGKAGAEHLACK
luteiventris ATNQC
Esculentin-2P Rana pipiens 37 GFSSIFRGVAKFASKGLGKDLARLGVNLVAC
KISKQC
Formaecin 1 Myrmecia 16 GRPNPVNNKPTPHPRL
gulosa
Formaecin 2 Myrmecia 16 GRPNPVNTKPTPYPRL
gulosa
Gaegurin-1 Rana rugosa 33 SLESLIKAGAKFLGKNLLKQGACYAACKASKQ
C
Gaegurin-2 Rana rugosa 33 GIMSIVKDVAKNAAKEAAKGALSTLSCKLAKT
C
Gaegurin-3 Rana rugosa 33 GIMSIVKDVAKTAAKEAAKGALSTLSCKLAKT
C
Gaegurin-4 Rana rugosa 80 MFTMKKSLLFLFFLGTISLSLCEEERSADEDD
precursor GGEMTEEEVKRGILDTLKQFAKGVGKDLVKG
AAQGVLSTVSCKLAKTC
Gaegurin-5 Rana rugosa 65 MFTLKKSLLLLFFLGTISLSLCEEERNADEEEK
precursor RDVEVEKRFLGALFKVASKVLPSVFCAITKKC
Gaegurin-6 Rana rugosa 24 FLPLLAGLAANFLPTIICKISYKC
Gal-1 alpha Gallus gallus 65 MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF
RKNGFCAFLKCPYLTLISGKCSRFHLCCKRIW
G
gallinacin Gallus gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF
YLCCKRIW
gallinacin Gallus gallus 36 LFCKGGSCHFGGCPSHLIKVGSCFGFRSCCK
WPWNA
Gallinacin 1 Gallus gallus 39 GRKSDCFRKNGFCAFLKCPYLTLISGKCSRF
alpha HLCCKRIW
Gallinacin 1 Gallus gallus 65 MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF
precursor RKSGFCAFLKCPSLTLISGKCSRFYLCCKRIW
G
Gallinacin 2 Gallus gallus 64 MRILYLLFSLLFLALQVSPGLSSPRRDMLFCK
precursor GGSCHFGGCPSHLIKVGSCFGFRSCCKWPW
NA
Gastric Sus scrofa 42 YAEGTFISDYSIAMDKIRQQDFVNWLLAQKG
inhibitory KKSDWKHNITQ
polypeptide
(GIP)
(Glucose-
dependent
insulinotropic
polypeptide)
Gloverin Hyalophora 130 DVTWDKNIGNGKVFGTLGQNDDGLFGKAGF
cecropia KQQFFNDDRGKFEGQAYGTRVLGPAGGTTN
FGGRLDWSDKNANAALDISKQIGGRPNLSAS
GAGVWDFDKNTRLSAGGSLSTMGRGKPDV
GVHAQFQHDF
Gomesin Acanthoscurria 18 QCRRLCYKQRCVTYCRGR
gomesiana
GP- Cavia 31 RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC
CS2 = CORTIC
OSTATIC
peptide
(Fragment)
Hadrurin Hadrurus 41 GILDTIKSIASKVWNSKTVQDLKRKGINWVAN
aztecus KLGVSPQAA
Hemiptericin Pyrrhocoris 133 DVELKGKGGENEGFVGLKAQRNLYEDDRTS
apterus LSGTVKGQSQWKDPYPAQHAGMARLDGTR
TLIENDRTKVTGSGFAQREVATGMRPHDSFG
VGVEATHNIYKGKNGEVDVFGGVQRQWNTP
DRHQARGGIRWRF
Hepcidin Mus 83 MALSTRTQAACLLLLLLASLSSTTYLQQQMR
antimicrobial musculus QTTELQPLHGEESRADIAIPMQKRRKRDINFP
peptide 2 ICRFCCQCCNKPSCGICCEE
hepcidin Danio rerio 91 MKLSNVFLAAVVILTCVCVFQITAVPFIQQVQ
antimicrobial DEHHVESEELQENQHLTEAEHRLTDPLVLFR
peptide TKRQSHLSLCRFCCKCCRNKGCGYCCKF
precursor
Hepcidin Morone 85 MKTFSVAVAVAVVLAFICLQESSAVPVTEVQE
precursor chrysops x LEEPMSNEYQEMPVESWKMPYNNRHKRHS
Morone SPGGCRFCCNCCPNMSGCGVCCRF
saxatilis
Hepcidin Mus 83 MALSTRTQAACLLLLLLASLSSTTYLHQQMR
precursor musculus QTTELQPLHGEESRADIAIPMQKRRKRDTNF
PICIFCCKCCNNSQCGICCKT
Hepcidin Rattus 84 MALSTRIQAACLLLLLLASLSSGAYLRQQTRQ
precursor norvegicus TTALQPWHGAESKTDDSALLMLKRRKRDTN
FPICLFCCKCCKNSSCGLCCIT
Hepcidin Oncorhynchus 61 LQVLTEEVGSIDSPVGEHQQPGGESMRLPE
precursor mykiss HFRFKRXSHLSLCRWCCNCCHNKGXGFCCK
(Fragment) F
Histone H2A Bufo 39 AGRGKQGGKVRAKAKTRSSRAGLQFPVGRV
[Contains: gargarizans HRLLRKGNY
Buforin I;
Buforin II]
(Fragment)
Histone H2A Hippoglossus 51 SGRGKTGGKARAKAKTRSSRAGLQFPVGRV
[Contains: hippoglossus HRLLRKGNYAHRVGAGAPVYL
Hipposin]
(Fragment)
Histone H2B-1 Ictalurus 20 PDPAKTAPKKGSKKAVTKXA
(Antibacterial punctatus
histone-like
protein 1)
(HLP-1)
(Fragment)
Histone H2B-3 Ictalurus 17 PDPAKTAPKKKSKKAVT
(Antibacterial punctatus
histone-like
protein 3)
(HLP-3)
(Fragment)
holotricin 1 Holotrichia 43 VTCDLLSLQIKGIAINDSACAAHCLAMRRKGG
diomphalia SCKQGVCVCRN
Holotricin 2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD
precursor diomphalia EADIEPQLSPAELHHGSIRERRSLQPGAPSFP
MPGSQLPTSVSGNVEKQGRNTIATIDAQHKT
DRYDVRGTWTKVVDGPGRSKPNFRIGGSYR
W
holotricin 2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD
precursor diomphalia EADIEPQLSPAELHHGSIRERRSLQPGAPSLS
QLPTSVSGNVEKQGRPMPGNTIATIDAQHKT
DRYDVRGTVDGPGRSKPNFRIGGSWTKVYR
W
Holotricin 3 Holotrichia 104 MNKLIILGLACIIAVASAMPYGPGDGHGGGHG
precursor diomphalia GGHGGGHGNGQGGGHGHGPGGGFGGGH
GGGHGGGGRGGGGSGGGGSPGHGAGGG
YPGGHGGGHHGGYQTHGY
Hymenoptaecin Apis mellifera 129 MKFIVLVLFCAVAYVSAQAELEPEDTMDYIPT
precursor RFRRQERGSIVIQGTKEGKSRPSLDIDYKQR
VYDKNGMTGDAYGGLNIRPGQPSRQHAGFE
FGKEYKNGFIKGQSEVQRGPGGRLSPYFGIN
GGFRF
Indolicidin Bos taurus 14 ILPWKWPWWPWRRX
Indolicidin Bos taurus 144 MQTQRASLSLGRWSLWLLLLGLVVPSASAQ
precursor ALSYREAVLRAVDQLNELSSEANLYRLLELDP
PPKDNEDLGTRKPVSFTVKETVCPRTIQQPA
EQCDFKEKGRVKQCVGTVTLDPSNDQFDLN
CNELQSVILPWKWPWWPWRRG
Insect Defensin Protophormia 40 ATCDLLSGTGINHSACAAHCLLRGNRGGYCN
A (NMR, 10 terraenovae GKGVCVCRN
Structures) -
Chai
Interferon- Mus sp. 15 SETAPAETPAPAKAE
activated
antimicrobial
protein
(Fragment)
Japonicin-1 Rana 14 FFPIGVFCKIFKTC
japonica
Japonicin-2 Rana 21 FGLPMLSILPKALCILLKRKC
japonica
Lactoferricin Bos taurus 25 FKCRRWQWRMKKLGAPSITCVRRAF
lactoferrin Sus scrofa 703 MKLFIPALLFLGTLGLCLAAPKKGVRWCVIST
precursor AEYSKCRQWQSKIRRTNPMFCIRRASPTDCI
RAIAAKRADAVTLDGGLVFEADQYKLRPVAA
EIYGTEENPQTYYYAVAWKKGFNFQNQLQG
RKSCHTGLGRSAGWNIPIGLLRRFLDWAGPP
EPLQKAVAKFFSQSCVPCADGNAYPNLCQL
CIGKGKDKCACSSQEPYFGYSGAFNCLHKGI
GDVAFVKESTVFENLPQKADRDKYELLCPDN
TRKPVEAFRECHLARVPSHAWARSVNGKE
NSIWELLYQSQKKFGKSNPQEFQLFGSPGQ
QKDLLFRDATIGFLKIPSKIDSKLYLGLPYLTAI
QGLRETAAEVEARQAKVVWCAVGPEELRKC
RQWSSQSSQNLNCSLASTTEDCIVQVLKGEA
DAMSLDGGFIYTAGKCGLVPVLAENQKSRQS
SSSDCVHRPTQGYFAVAWRKANGGITWNS
VRGTKSCHTAVDRTAGWNIPMGLLVNQTGS
CKFDEFFSQSCAPGSQPGSNLCALCVGNDQ
GVDKCVPNSNERYYGYTGAFRCLAENAGDV
AFVKDVTVLDNTNGQNTEEWARELRSDDFE
LLCLDGTRKPVTEAQNCHLAVAPSHAWSRK
EKAAQVEQVLLTEQAQFGRYGKDCPDKFCL
FRSETKNLLFNDNTECLAQLQGKTTYEKYLG
SEYVTAIANLKQCSVSPLLEACAFMMR
Lactotransferrin Bos taurus 708 MKLFVPALLSLGALGLCLAAPRKNVRWCTIS
precursor QPEWFKCRRWQWRMKKLGAPSITCVRRAF
(Lactoferrin) ALECIRAIAEKKADAVTLDGGMVFEAGRDPY
[Contains: KLRPVAAEIYGTKESPQTHYYAVAVVKKGSN
Lactoferricin B FQLDQLQGRKSCHTGLGRSAGWIIPMGILRP
(LFCIN B)] YLSWTESLEPLQGAVAKFFSASCVPCIDRQA
YPNLCQLCKGEGENQCACSSREPYFGYSGA
FKCLQDGAGDVAFVKETTVFENLPEKADRDQ
YELLCLNNSRAPVDAFKECHLAQVPSHAWA
RSVDGKEDLIWKLLSKAQEKFGKNKSRSFQL
FGSPPGQRDLLFKDSALGFLRIPSKVDSALYL
GSRYLTTLKNLRETAEEVKARYTRVVWCAVG
PEEQKKCQQWSQQSGQNVTCATASTTDDCI
VLVLKGEADALNLDGGYIYTAGKCGLVPVLAE
NRKSSKHSSLDCVLRPTEGYLAVAWKKANE
GLTWNSLKDKKSCHTAVDRTAGWNIPMGLIV
NQTGSCAFDEFFSQSCAPGADPKSRLCALC
AGDDQGLDKCVPNSKEKYYGYTGAFRCLAE
DVGDVAFVKNDTVWENTNGESTADWAKNLN
REDFRLLCLDGTRKPVTEAQSCHLAVAPNHA
VVSRSDRAAHVKQVLLHQQALFGKNGKNCP
DKFCLFKSETKNLLFNDNTECLAKLGGRPTY
EEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
Lebocin 1/2 Bombyx mori 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP
precursor TQRPIIRTARQAGQEPLWLYQGDNVPRAPST
ADHPILPSKIDDVQLDPNRRYVRSVTNPENN
EASIEHSHHTVDTGLDQPIESHRNTRDLRFLY
PRGKLPVPTPPPFNPKPIYIDMGNRYRRHAS
DDQEELRQYNEHFLIPRDIFQE
Lebocin 3 Bombyx mori 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP
precursor (LEB TQRPITRTVRQAGQEPLWLYQGDNVPRAPS
3) TADHPILPSKIDDVQLDPNRRYVRSVTNPENN
EASIEHSHHTVDIGLDQPIESHRNTRDLRFLY
PRGKLPVPTLPPFNPKPIYIDMGNRYRRHAS
EDQEELRQYNEHFLIPRDIFQE
lectin-L6 Limulus 221 VQWHQIPGKLMHITATPHFLWGVNSNQQIYL
polyphemus CRQPCYDGQWTQISGSLKQVDADDHEVWG
VNRNDDIYKRPVDGSGSVVVRVSGKLKHVSA
SGYGYIWGVNSNDQIYKCPKPCNGAWTQVN
GRLKQIDGGQSMVYGVNSANAIYRRPVDGS
GSWQQISGSLKHITGSGLSEVFGVNSNDQIY
RCTKPCSGQWSLIDGRLKQCDATGNTIVGVN
SVDNIYRSG
Limulus factor Tachypleus 394 MKVLLLVAFLLGTTLAYPQDDDGPVWGGSS
D tridentatus NDNDDGGISSRVGNPQSGFGNCECVPYYLC
KDNNIIIDGSGLLDPRKKPVASKEPKLSARLG
PEGPSGCGPFHVCCIAPETSTVKPYTHQCGF
RNVNGINKRILSPNGKDLSEFGEWPWQGAVL
KVEGKVNIFQCGAVLIDSYHLLTVAHCVYKFT
LENAFPLKVRLGEWDTQNTNEFLKHEDYEVE
KIYIHPKYDDERKNLWDDIAILKLKAEVSFGPH
IDTICLPNNQEHFAGVQCVVTGWGKNAYKNG
SYSNVLREVHVPVITNDRCQELLRKTRLSEW
YVLYENFICAGGESNADSCKGDGGGPLTCW
RKDGTYGLAGLVSWGINCGSPNVPGVYVRV
SNYLDWITKITGRPISDYWPRS
Lingual Bos taurus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNSQSC
antimicrobial RRNKGICVPIRCPGSMRQIGTCLGAQVKCCR
peptide RK
precursor
Liver- Bos taurus 77 MWHLKLFAVLMICLLLLAQVDGSPIPQQSSAK
expressed RRPRRMTPFWRAVSLRPIGASCRDDSECITR
antimicrobial LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver- Macaca 77 MWHLKLCAVLMIFLLLLGQTDGSPIPEVSSAK
expressed mulatta RRPRRMTPFWRGVSLRPIGASCRDDSECITR
antimicrobial LCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver- Mus 76 MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAK
expressed musculus RSRRMTPFWRGVSLRPIGASCRDDSECITRL
antimicrobial CRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver- Sus scrofa 77 MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK
expressed RRPRRMTPFWRAVSLRPIGASCRDDSECLT
antimicrobial RLCRKRRCSLSVAQE
peptide 2
precursor
(LEAP-2)
Liver- Cavia 71 SVVLLICLLLLGQVDGSPVPEKSSVKKRLRRM
expressed porcellus TPFWRGVSLRPIGASCRDDSECITRLCKKRR
antimicrobial CSLSVAQE
peptide 2
precursor
(LEAP-2)
(Fragment)
Liver- Sus scrofa 77 MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK
expressed RRPRRITPFWRAVSLRPIGASCRDDSECLTR
antimicrobial LCRKRRCSLSVAQE
protein 2
Lysozyme Heliothis 141 MQKLTLFVVALAAVVLHCEAKQFSRCGLVQE
virescens LRRQGFPEDKLGDWVCLVENESARKTDKVG
TVNKNGSRDYGLYQINDKYWCSNTSTPGKD
CNVTCAEMLLDDITKASTCAKKIYKRHKFEAW
YGWKNHCKGKTLPDISNC
lysozyme (EC Alopochen 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17) aegyptiacus AAKYESGFNTQATNRNTDGSTDYGILQINSR
WWCNDGKTPRAKNVCGIPCSVLLRSDITEAV
KCAKRIVSDGNGMNAWVAWRNRCKGTDVS
QWIRGCRL
lysozyme (EC Chrysolophus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17) pictus AAKFESNFNTHATNRNTDGSTDYGILQINSR
WWCNDGRTPGSRNLCHIPCSALLSSDITASV
NCAKKIVSDGNGMNAWVAWRNRCKGTDVN
AWTRGCRL
lysozyme (EC Lophophorus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
3.2.1.17) impejanus AAKFESNFNTHATNRNTDGSTDYGILQINSR
WWCNDGRTPGSRNLCNIPCSALLSSDITASV
NCAKKIVSDGNGMNAVWAWRNRCKGTDVH
AWIRGCRL
lysozyme (EC Manduca 120 KHFSRCELVHELRRQGFPENLMRDWVCLVE
3.2.1.17) sexta NESSRYTDKVGRVNKNGSRDYGLFQINDKY
WCSNGSTPGKDCNVKCSDLLIDDITKASTCA
KKIYKRHKFQAWYGWRNHCQGSLPDISSC
lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 1 TKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENNIAKA
VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCSL
lysozyme (EC Rattus 148 MKALLVLGFLLLSASVQAKIYERCEFARTLKR
3.2.1.17) 1 norvegicus NGMSGYYGVSLADWVCLAQHESNYNTQAR
precursor NYNPGDQSTDYGIFQINSRYWCNDGKTPRA
KNACGIPCSALLQDDITQAIQCAKRVVRDPQ
GIRAWVAWQRHCKNRDLSGYIRNCGV
lysozyme (EC Bos taurus 129 KTFKRCELARTLKNLGLAGYKGVSLANWMCL
3.2.1.17) 14d, AKGESNYNTQAKNYNPGSKSTDYGIFQINSK
tracheal WWCNDGKTPKAVNGCGVSCSALLKDDITQA
VACAKKIVSQQGITAWVAWKNKCRNRDLTSY
VKGCGV
lysozyme (EC Cervus axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2 TKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVACSELMENDIAKA
VACAKQIVREQGITAWVAWKSHCRDHDVSS
YVEGCTL
lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2 TKWESSYNTKATNYNPGSESTDYGIEQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKA
VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
lysozyme (EC Ovis aries 129 KVFERCELARTLKKLGLDDYKGVSLANWLCL
3.2.1.17) 3 TKWESGYNTKATNYNPGSESTDYGIEQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKA
VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL
lysozyme (EC Bos taurus 130 KVFERCELARSLKRFGMDNFRGISLANWMCL
3.2.1.17) 5a, ARWESNYNTQATNYNAGDQSTDYGIEQINSH
tracheal WWCNDGKTPGAVNACHLPCGALLQDDITQA
VACAKRWSDPQGIRAWVAWRSHCQNQDLT
SYIQGCGV
lysozyme (EC Drosophila 140 MKAFIVLVALASGAPALGRTMDRCSLAREMS
3.2.1 .17) B melanogaster NLGVPRDQLARWACIAEHESSYRTGVVGPE
precursor NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF
lysozyme (EC Papio sp. 130 KIFERCELARTLKRLGLDGYRGISLANWVCLA
3.2.1.17) c KWESDYNTQATNYNPGDQSTDYGIEQINSHY
WCNDGKTPGAVNACHISCNALLQDNITDAVA
CAKRVVSDPQGIRAWVAWRNHCQNRDVSQ
YVQGCGV
lysozyme (EC Numida 129 KVFGRCELAAAMKRHGLDNYRGYSLGNWVC
3.2.1.17) c meleagris AAKFESNFNSQATNRNTDGSTDYGVLQINSR
[validated] WWCNDGRTPGSRNLCNIPCSALQSSDITATA
NCAKKIVSDGDGMNAWVAWRKHCKGTDVR
VWIKGCRL
lysozyme (EC Coturnix 129 KVYGRCELAAAMKRHGLDKYQGYSLGNWV
3.2.1.17) C japonica CAAKFESNFNTQATNRNTDGSTDYGILQINS
precursor RWWCNDGRTPGSRNLCNIPCSALLSSDITAS
VNCAKKIVSDVHGMNAWVAWRNRCKGTDV
NVWIRGCRL
lysozyme (EC Hyalophora 132 CRSWQFALHCDAKRFTRCGLVQELRRRGFD
3.2.1.17) c cecropia ETLMSNWVCLVENESGRFTDKIGKVNKNGS
precursor RDYGLFQINDKYWCSKGSTPGKDCNVTCNQ
LLTDDISVAATCAKKIYKRHKFDAWYGWKNH
CQHGLPDISDC
lysozyme (EC Phasianus 147 MRSLLILVLCFLPLAAPGKVYGRCELAAAMKR
3.2.1.17) c colchicus MGLDNYRGYSLGNVWCAAKFESNFNTGATN
precursor RNTDGSTDYGILQINSRWWCNDGRTPGSKN
[validated] LCHIPCSALLSSDITASVNCAKKIVSDGDGMN
AWVAWRKHCKGTDVNVWIRGCRL
lysozyme (EC Drosophila 140 MKAFIVLVALALAAPALGRTLDRCSLAREMSN
3.2.1.17) E melanogaster LGVPRDQLARWACIAEHESSYRTGWGPEN
precursor YNGSNDYGIFQINDYYWCAPPSGRFSYNEC
GLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF
lysozyme (EC Rhea 185 RTNCYGDVSRIDTTGASCKTAKPEKLNYCGV
3.2.1.17) g americana AASRKIAERDLRSMDRYKTLIKKVGQKLCVEP
AVIAGIISRESHAGKALKNGWGDNGNGFGLM
QVDRRSHKPVGEWNGERHLIQGTEILISMIKA
MQRKFPRWTKEQQLKGGISAYNAGPGNVRT
YERMDIGTTHDDYANDVVARAQYYKQHGY
lysozyme (EC Casuarius 185 QTGCYGWNRIDTTGASCETAKPEKLNYCGV
3.2.1.17) g casuarius AASRKIAEGDLQSMDRYKTLIKKVGQKLCVD
[validated] PAVIAGIISRESHAGKALKDGWGDNGNGFGL
MQVDKRSHTPVGKWNGERHLTQGTEILISMI
KKIQKKFPRWTKEQQLKGGISAYNAGSGNVR
TYERMDIGTTHNDYANDVVARAQYYKQHGY
lysozyme (EC Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMS
3.2.1.17) melanogaster NLGVPRDQLNKWACIAEHESSYRTGVVGPE
precursor NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF
lysozyme (EC Opisthocomus 145 MLFFGFLLAFLSAVPGTEGEIISRCELVKILRE
3.2.1.17) hoazin HGFEGFEGTTIADWICLVQHESDYNTEAYNN
precursor, NGPSRDYGIFQINSKYWCNDGKTSGAVDGC
stomach HISCSELMTNDLEDDIKCAKKIARDAHGLTPW
YGWKNHCEGRDLSSYVKGC
lysozyme (EC Drosophila 139 MKAFFALVLLPLPLCLAGRTLDRCSLAREMA
3.2.1.17) S melanogaster DLGVPRDQLDKWTCIAQHESDYRTWVVGPA
precursor NSDGSNDYGIFQINDLYWCQADGRFSYNEC
GLSCNALLTDDITNSVRCAQKVLSQQGWSA
WAVWHYCSGWLPSIDECF
lysozyme (EC Drosophila 81 PNTDGSNDYGIFQINDLYWCQPSSGKFSHN
3.2.1.17) X melanogaster GCDVSCNALLTDDIKSSVRCALKVLGQQGW
SAWSTWHYCSGYLPPIDDCFV
Lysozyme Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMS
A/C/D melanogaster NLGVPRDQLARWACIAEHESSYRTGVVGPE
precursor (EC NYNGSNDYGIFQINDYYWCAPPSGRFSYNE
3.2.1.17) (1,4- CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
beta-N- WSTWHYCSGWLPSIDDCF
acetylmurami-
dase A/C)
Lysozyme C Callipepla 129 KVFGRCELAAAMKRHGLDNYRGYSLGNWVC
(EC 3.2.1.17) californica AAKFESNFNSQATNRNTDGSTDYGVLQINSR
(1,4-beta-N- WWCNDGRTPGSRNLCNIPCSALLSSDITATV
acetylmurami- NCAKKIVSDGNGMNAWVAWRNRCKGTDVH
dase C) AWIRGCRL
Lysozyme C Colinus 130 MKVFGRCELAAAMKRHGLDNYRGYSLGNW
(EC 3.2.1.17) virginianus VCAAKFESNFNSQATNRNTDGSTDYGVLQIN
(1,4-beta-N- SRWWCNDGKTPGSRNLCNIPCSALLSSDITA
acetylmurami- TVNCAKKIVSDGNGMNAWVAWRNRCKGTD
dase C) VQAWIRGCRL
Lysozyme C Columba livia 127 KDIPRCELVKILRRHGFEGFVGKTVANWVCL
(EC 3.2.1.17) VKHESGYRTTAFNNNGPNSRDYGIFQINSKY
(1,4-beta-N- WCNDGKTRGSKNACNINCSKLRDDNIADDIQ
acetylmurami- CAKKIAREARGLTPWVAWKKYCQGKDLSSY
dase C) VRGC
Lysozyme C Equus asinus 129 KVFSKCELAHKLKAQEMDGFGGYSLANWVC
(EC 3.2.1.17) MAEYESNFNTRAFNGKNANGSYDYGLFQLN
(1,4-beta-N- SKWWCKDNKRSSSNACNIMCSKLLDDNIDD
acetylmurami- DISCAKRVVRDPKGMSAWKAWVKHCKDKDL
dase C) SEYLASCNL
Lysozyme C Ortalis vetula 129 KIYKRCELAAAMKRYGLDNYRGYSLGNWVC
(EC 3.2.1.17) AARYESNYNTQATNRNSNGSTDYGILQINSR
(1,4-beta-N- WWCNDGRTPGTKNLCHISCSALMGADIAPS
acetylmurami- VRCAKRIVSDGDGMNAWVAWRKHCKGTDV
dase C) STWIKDCKL
Lysozyme C Oryctolagus 130 KIYERCELARTLKKLGLDGYKGVSLANWMCL
(EC 3.2.1.17) cuniculus AKWESSYNTRATNYNPGDKSTDYGIFQINSR
(1,4-beta-N- YWCNDGKTPRAVNACHIPCSDLLKDDITQAV
acetylmurami- ACAKRWSDPQGIRAWVAWRNHCQNQDLTP
dase C) YIRGCGV
Lysozyme C Syrmaticus 129 KVYGRCELAAAMKRLGLDNFRGYSLGNWVC
(EC 3.2.1.17) soemmerringii AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N- WWCNDGRTPGSRNLCNIPCSALLSSDTIASV
acetylmurami- NCAKKIVSDGNGMNAWVAWRKRCKGTDVN
dase C) (CPL) AWTRGCRL
Lysozyme C Felis catus 20 KIFTKCELARKLRAEGMDGF
(EC 3.2.1.17)
(1,4-beta-N-
acetylmurami-
dase C)
(Fragment)
Lysozyme C Pseudocheirus 49 SKMKKCEFAKIAKEQHMDGYHGVSLADWVC
(EC 3.2.1.17) peregrinus LVNNESDFNTKAINRNKGI
(1,4-beta-N-
acetylmurami-
dase C)
(Fragment)
Lysozyme C Lophura 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVNC
(EC 3.2.1.17) leucomelanos AAKYESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N- WWCNDGKTPGSRNLCHIPCSALLSSDITASV
acetylmurami- NCAKKIVSDGNGMNAWVAWRNRCKGTDVS
dase) VWTRGCRL
Lysozyme C Pavo 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17) cristatus AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N- WWCNDGRTPGSRNLCNIPCSALLSSDITASV
acetylmurami- NCAKKIVSDRNGMNAWVAWRNRCKGTDVH
dase) AWIRGCRL
Lysozyme C Phasianus 130 GKVYGRCELAAAMKRMGLDNYRGYSLGNW
(EC 3.2.1.17) versicolor VCAAKFESNFNTGATNRNTDGSTDYGILQIN
(1,4-beta-N- SRWWCNDGRTPGSKNLCHIPCSALLSSDITA
acetylmurami- SVNCAKKIVSDGDGMNAWVAWRKHCKGTD
dase) VNVWIRGCRL
Lysozyme C Syrmaticus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17) reevesi AAKFESNFNTHATNRNTDGSTDYGILQINSR
(1,4-beta-N- WWCNDGRTPGSRNLCHISCSALLSSDITASV
acetylmurami- NCAKKIVSDRNGMNAWVAWRNRCKGTDVN
dase) AWIRGCRL
Lysozyme C 1 Cervus axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
and 2 (EC TKWESSYNTKATNYNPGSESTDYGIFQINSK
3.2.1.17) (1,4- WWCDDGKTPNAVDGCHVACSELMENNIDKA
beta-N- VTCAKQIVREQGITAWVAWKSHCRGHDVSS
acetylmurami- YVEGCTL
dase C)
Lysozyme C 1 Bos taurus 147 MKALIILGFLFLSVAVQGKVFERCELARTLKKL
precursor (EC GLDGYKGVSLANWLCLTKWESSYNTKATNY
3.2.1.17) (1,4- NPGSESTDYGIFQINSKWWCNDGKTPNAVD
beta-N- GCHVSCSELMENDIAKAVACAKQIVSEQGITA
acetylmurami- WVAWKSHCRDHDVSSYVEGCTL
dase C)
Lysozyme C 2 Bos taurus 147 MKALVILGFLFLSVAVQGKVFERCELARTLKK
precursor (EC LGLDGYKGVSLANWLCLTKWESSYNTKATN
3.2.1.17) (1,4- YNPSSESTDYGIFQINSKWWCNDGKTPNAV
beta-N- DGCHVSCSELMENDIAKAVACAKHIVSEQGIT
acetylmurami- AWVAWKSHCRDHDVSSYVEGCTL
dase C)
Lysozyme C 3 Bos taurus 147 MKALIILGFLFLSVAVQGKVFERCELARTLKKL
precursor (EC GLDGYKGVSLANWLCLTKWESSYNTKATNY
3.2.1.17) (1,4- NPSSESTDYGIFQINSKWWCNDGKTPNAVD
beta-N- GCHVSCSELMENDIAKAVACAKHIVSEQGITA
acetylmurami- WVAWKSHCRDHDVSSYVQGCTL
dase C)
Lysozyme C I Tachyglossus 125 KILKKQELCKNLVAQGMNGYQHITLPNWVCT
(EC 3.2.1.17) aculeatus AFHESSYNTRATNHNTDGSTDYGILQINSRY
(1,4-beta-N- WCHDGKTPGSKNACNISCSKLLDDDITDDLK
acetylmurami- CAKKIAGEAKGLTPWVAWKSKCRGHDLSKF
dase C) KC
Lysozyme C II Oncorhynchus 144 MRAVVVLLLVAVASAKVYDRCELARALKASG
precursor (EC mykiss MDGYAGNSLPNWVCLSKWESSYNTQATNR
3.2.1.17) (1,4- NTDGSTDYGIFQINSRYWCDDGRTPGAKNV
beta-N- CGIRCSQLLTADLTVAIRCAKRWLDPNGIGA
acetylmurami- WVAWRLHCQNQDLRSYVAGCGV
dase C)
Lysozyme C Coturnix 147 MRSLLVLVLCFLPLAALGKVYGRCELAAAMK
precursor (EC japonica RHGLDKYQGYSLGNWVCAAKFESNFNTQAT
3.2.1.17) (1,4- NRNTDGSTDYGILQINSRWWCNDGRTPGSR
beta-N- NLCNIPCSALLSSDITASVNCAKKIVSDVHGM
acetylmurami- NAWVAWRNRCKGTDVNAWIRGCRL
dase C)
Lysozyme C Meleagris 147 MRSLLILVLCFLPLAALGKVYGRCELAAAMKR
precursor (EC gallopavo LGLDNYRGYSLGNWVCAAKFESNFNTHATN
3.2.1.17) (1,4- RNTDGSTDYGILQINSRWWCNDGRTPGSKN
beta-N- LCNIPCSALLSSDITASVNCAKKIASGGNGMN
acetylmurami- AWVAWRNRCKGTDVHAWIRGCRL
dase C)
Lysozyme C Presbytis 148 MKALTILGLVLLSVTVQGKIFERCELARTLKKL
precursor (EC entellus GLDGYKGVSLANWVCLAKWESGYNTEATNY
3.2.1.17) (1,4- NPGDESTDYGIFQINSRYWCNNGKTPGAVD
beta-N- ACHISCSALLQNNIADAVACAKRVVSDPQGIR
acetylmurami- AWVAWRNHCQNKDVSQYVKGCGV
dase C)
Lysozyme C Gallus gallus 147 MRSLLILVLCFLPLAALGKVFGRCELAAAMKR
precursor (EC HGLDNYRGYSLGNWVCAAKFESNFNTQATN
3.2.1.17) (1,4- RNTDGSTDYGILQINSRWWCNDGRTPGSRN
beta-N- LCNIPCSALLSSDITASVNCAKKIVSDGNGMN
acetylmurami- AWVAWRNRCKGTDVQAWIRGCRL
dase C)
(Allergen Gal d
4) Gal d IV)
Lysozyme C, Rattus 148 MKALLVLGFLLLSASVQAKVFKHCELARILRS
type 2 norvegicus SALAGYRGVSLENWMCMAQHESNFDTEAIN
precursor (EC YNSTDQSTDYGIFQINSRYWCNDGKTPRAVN
3.2.1.17) (1,4- AGGIPCSALLQDDITQAIQCAKRVVRDPQGIR
beta-N- AWVAWQRHCQNRDLSGYIRNCGV
acetylmurami-
dase C)
Lysozyme C, Mus 148 MKTLLTLGLLLLSVTAQAKVYERCEFARTLKR
type M musculus NGMAGYYGVSLADWVCLAQHESNYNTRATN
precursor (EC YNRGDQSTDYGIFQINSRYWCNDGKTPRAV
3.2.1.17) (1,4- NACGINCSALLQDDITAAIQCAKRWRDPQGI
beta-N- RAWVAWRAHCQNRDLSQYIRNCGV
acetylmurami-
dase C)
Lysozyme C, Mus 148 MKALLTLGLLLLSVTAQAKVYNRCELARILKR
type P musculus NGMDGYRGVKLADWVCLAQHESNYNTRAT
precursor (EC NYNRGDRSTDYGIFQINSRYWCNDGKTPRS
3.2.1.17) (1,4- KNACGINCSALLQDDITAAIQCAKRVVRDPQG
beta-N- IRAWVAWRTQCQNRDLSQYIRNCGV
acetylmurami-
dase C)
Lysozyme C-1 Anas 147 MKALLTLVFCLLPLAAQGKVYSRCELAAAMK
precursor (EC platyrhynchos RLGLDNYRGYSLGNWVCAANYESGFNTQAT
3.2.1.17) (1,4- NRNTDGSTDYGILQINSRWWCDNGKTPRSK
beta-N- NACGIPCSVLLRSDITEAVRCAKRIVSDGDGM
acetylmurami- NAWVAWRNRCRGTDVSKWIRGCRL
dase C)
Lysozyme C-3 Anas 129 KVYERCELAAAMKRLGLDNYRGYSLGNWVC
(EC 3.2.1.17) platyrhynchos AANYESSFNTQATNRNTDGSTDYGILEINSR
(1,4-beta-N- WWCDNGKTPRAKNACGIPCSVLLRSDITEAV
acetylmurami- KCAKRIVSDGDGMNAWVAWRNRCKGTDVS
dase) RWIRGCRL
Lysozyme G Anser anser 185 RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV
(EC 3.2.1.17) SASKKIAERDLQAMDRYKTIIKKVGEKLCVEP
(1,4-beta-N- AVIAGIISRESHAGKVLKNGWGDRGNGFGLM
acetylmurami- QVDKRSHKPQGTWNGEVHITQGTTILINFIKTI
dase) (Goose- QKKFPSWTKDQQLKGGISAYNAGAGNVRSY
type lysozyme) ARMDIGTTHDDYANDVVARAQYYKQHGY
Lysozyme G Cygnus 185 RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV
(EC 3.2.1.17) atratus PASKTIAERDLKAMDRYKTIIKKVGEKLCVEP
(1,4-beta-N- AVIAGIISRESHAGKVLKNGWGDRGNGFGLM
acetylmurami- QVDKRSHKPQGTWNGEVHITQGTTILTDFIK
dase) (Goose- RIQKKFPSWTKDQQLKGGISAYNAGAGNVRS
type lysozyme) YARMDIGTTHDDYANDVVARAQYYKQHGY
Lysozyme G Struthio 185 RTGCYGDVNRVDTTGASCKSAKPEKLNYCG
(EC 3.2.1.17) camelus VAASRKIAERDLQSMDRYKALIKKVGQKLCV
(1,4-beta-N- DPAVIAGIISRESHAGKALRNGWGDNGNGFG
acetylmurami- LMQVDRRSHKPVGEWNGERHLMQGTEILIS
dase) (Goose- MIKAIQKKFPRWTKEQQLKGGISAYNAGPGN
type lysozyme) VRSYERMDIGTTHDDYANDVVARAQYYKQH
GY
Lysozyme G Gallus gallus 211 MLGKNDPMCLVLVLLGLTALLGICQGGTGCY
precursor (EC GSVSRIDTTGASCRTAKPEGLSYCGVRASRT
3.2.1.17) (1,4- IAERDLGSMNKYKVLIKRVGEALCIEPAVIAGII
beta-N- SRESHAGKILKNGWGDRGNGFGLMQVDKRY
acetylmurami- HKIEGTWNGEAHIRQGTRILIDMVKKIQRKFP
dase) (Goose- RWTRDQQLKGGISAYNAGVGNVRSYERMDI
type lysozyme) GTLHDDYSNDVVARAQYFKQHGY
Lysozyme P Drosophila 141 MKAFLVICALTLTAVATQARTMDRCSLAREM
precursor (EC melanogaster SKLGVPRDQLAKWTCIAQHESSFRTGVVGPA
3.2.1.17) (1,4- NSNGSNDYGIFQINNKYWCKPADGRFSYNE
beta-N- CGLSCNALLTDDITNSVKCARKIQRQQGWTA
acetylmurami- WSTWKYCSGSLPSINSCF
dase P)
Lysozyme Chlamys 137 MMYFVLLCLLATGTTYGAHNFATGIVPQSCL
precursor islandica ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ
AYWEDCGRPGGSLTSCADDIHCSSQCVQHY
MSRYIGHTSCSRTCESYARLHNGGPHGCEH
GSTLGYWGHVQGHGC
Lysozyme Bombyx mori 137 MQKLIIFALWLCVGSEAKTFTRCGLVHELRK
precursor (EC HGFEENLMRNWVCLVEHESSRDTSKTNTNR
3.2.1.17) (1,4- NGSKDYGLFQINDRYWCSKGASPGKDCNVK
beta-N- CSDLLTDDITKAAKCAKKIYKRHRFDAWYGW
acetylmurami- KNHCQGSLPDISSC
dase)
Lysozyme Hyalophora 139 MTKYVILLAVLAFALHCDAKRFTRCGLVQELR
precursor (EC cecropia RLGFDETLMSNWVCLVENESGRFTDKIGKVN
3.2.1.17) (1,4- KNGSRDYGLFQINDKYWCSKGTTPGKDCNV
beta-N- TCNQLLTDDISVAATCAKKIYKRHKFDAWYG
acetylmurami- WKNHCQHGLPDISDC
dase)
Maculatin 1.1 Litoria 21 GLFGVLAKVAAHVVPAIAEHF
[Contains: genimaculata
Maculatin
1.1.1]
Maculatin 1.2 Litoria 23 GLFGVLAKVASHVVPAIAEHFQA
genimaculata
Maculatin 2.1 Litoria 18 GFVDFLKKVAGTIANVVT
genimaculata
Maculatin 3.1 Litoria 26 GLLQTIKEKLESLESLAKGIVSGIQA
genimaculata
Magainins Xenopus 303 MFKGLFICSLIAVICANALPQPEASADEDMDE
precursor laevis REVRGIGKFLHSAGKFGKAFVGEIMKSKRDA
EAVGPEAFADEDLDEREVRGIGKFLHSAKKF
GKAFVGEIMNSKRDAEAVGPEAFADEDLDER
EVRGIGKFLHSAKKFGKAFVGEIMNSKRDAE
AVGPEAFADEDLDEREVRGIGKFLHSAKKFG
KAFVGEIMNSKRDAEAVGPEAFADEDFDERE
VRGIGKFLHSAKKFGKAFVGEIMNSKRDAEA
VGPEAFADEDLDEREVRGIGKFLHSAKKFGK
AFVGEIMNSKRDAEAVDDRRWVE
Melittin-like Rana 22 FIGSALKVLAGVLPSIVSWVKQ
peptide (MLP) temporaria
Metchnikowin Drosophila 52 MQLNLGAIFLALLGVMATTTSVLAEPHRRQG
melanogaster PIFDTRPSPFNPNQPRPGPIY
Metchnikowin Drosophila 52 MQLNLGAIFLALLGVMATATSVLAEPHRHQG
precursor melanogaster PIFDTRPSPFNPNQPRPGPIY
MGD1 Mytilus 57 CPNNYQCHRHCKSIPGRCGGYCGGWHRLR
antimicrobial galloprovincialis CTCYRCGGRREDVEDIEDIFDNEAADRF
peptide
(Fragment)
Misgurin Misgurnus 21 RQRVEELSKFSKKGAAARRRK
anguillicaudatus
Moricin 1 Bombyx mori 66 MNILKFFFVFIVAMSLVSCSTAAPAKIPIKAIKT
precursor VGKAVGKGLRAINIASTANDVENFLKPKKRKH
Moricin 2 Bombyx mori 66 MNILKLFFVFIVAMSLVSCSTAAPAKIPIKAIKT
precursor VGKAVGKGLRAINIASTANDVENFLKPKKRKH
myeloid Ovis aries 160 METQRASLSLGRRSLWLLLLGLVLASARAQA
antimicrobial LSYREAVLRAVDQLNEKSSEANLYRLLELDP
peptide 29 PPKQDDENSNIPKPVSFRVKETVCPRTSQQP
precursor AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
RIAG
Myeloid Ovis aries 165 METQRAGLSLGRWSLRLLLLGLVLPSASTRS
antimicrobial FSYREAVLRAVDQFNERSAEANLYRLLELDP
peptide PPEQDAEDRGARKPVSFKVKETVCPRTSQQ
precursor PVEQCDFRKNGLVKQCVGTVTRYWIRGDFDI
TCKDIQNVGLFGRLRDSLQRGGQKILEKAERI
GDRIKDIFRG
Myticin A Mytilus 96 MKATILLAVLVAVFVAGTEAHSHACTSYWCG
precursor galloprovincialis KFCGTASCTHYLCRVLHPGKMCACVHCSRV
NNPFRVNQVAKSINDLDYTPIMKSMENLDNG
MDML
Myticin B Mytilus 96 MKATMLLAVVVAVFVAGTEAHPHVCTSYYCS
precursor galloprovincialis KFCGTAGCTRYGCRNLHRGKLCFCLHCSRV
KFPFGATQDAKSMNELEYTPIMKSMENLDNG
MDML
Mytilin A Mytilus edulis 34 GCASRCKAKCAGRRCKGWASASFRGRCYC
KCFRC
Mytilin B Mytilus edulis 34 SCASRCKGHCRARRCGYYVSVLYRGRCYCK
CLRC
Mytilin B Mytilus 103 MKAAVILAIALVAILAVHEAEASCASRCKGHC
antimicrobial galloprovincialis RARRCGYYVSVLYRGRCYCKCLRCSSEHSM
peptide KFPENEGSSPSDMMPQMNENENTEFGQDM
precursor PTGETEQGETGI
Mytimycin Mytilus edulis 33 DCCRKPFRKHCWDCTAGTPYYGYSTRNIFG
(Fragment) CTC
Neutrophil Rattus 94 MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ
antibiotic norvegicus EQLVMEDQDISISFGGDKGTALQDADVKAGV
peptide NP-1 TCYCRRTRCGFRERLSGACGYRGRIYRLCC
precursor R
(Neutrophil
defensin 1)
(RatNP-1)
Neutrophil Rattus 94 MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ
antibiotic norvegicus EQLVMEDQDISISFGGDKGTALQDADVKAGV
peptide NP-2 TCYCRSTRCGFRERLSGACGYRGRIYRLCC
precursor R
(Neutrophil
defensin 2)
(RatNP-2)
Neutrophil Rattus 87 MRTLTLLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic norvegicus EQDISVFFGGDKGTALQDAAVKAGVTCSCRT
peptide NP-3 SSCRFGERLSGACRLNGRIYRLCC
precursor
(Neutrophil
defensin 3)
(RatNP-3a)
Neutrophil Rattus 87 MRTLILLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic norvegicus EQDISVFFGGDKGTALQDAAVKAGVTCSCRT
peptide NP-3 SSCRFGERLSGACRLNGRIYRLCC
precursor
(Neutrophil
defensin 3)
(RatNP-3b)
Neutrophil Oryctolagus 95 MRTLALLAAILLVTLQAQAELHSGMADDGVD
antibiotic cuniculus QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG
peptide NP-4 VSCTCRRFSCGFGERASGSCTVNGVRHTLC
precursor CRR
(Microbicidal
peptide NP-4)
Neutrophil Rattus 93 MRTLTLLITLLLLALHTQAESPQERAKAAPDQ
antibiotic norvegicus DMVMEDQDIFISFGGYKGTVLQDAVVKAGQA
peptide NP-4 CYCRIGACVSGERLTGACGLNGRIYRLCCR
precursor
(Neutrophil
defensin 4)
(RatNP-4)
Neutrophil Oryctolagus 95 MRTLALLAAILLVTLQAQAELHSGMADDGVD
antibiotic cuniculus QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG
peptide NP-5 VFCTCRGFLCGSGERASGSCTINGVRHTLCC
precursor RR
(Microbicidal
peptide NP-5)
neutrophil beta- Bos taurus 60 MRLHHLLLALLFLVLSAASGISGPLSCGRNGG
defensin 12 VCIPIRCPVPMRQIGTCFGRPVKCCRSW
neutrophil beta- Bos taurus 54 MRLHHLLLVLLFLVLSAGSGFTQWRNPQSC
defensin 5 RWNMGVCIPISCPGNMRQIGTCS
Neutrophil Cavia 178 MGTPRDAASGGPRLLLPLLLLLLLTPATAWVL
cationic porcellus SYQQAVQRAVDGINKNLADNENLFRLLSLDT
antibacterial QPPGDNDPYSPKPVSFTIKETVCTKMLQRPL
polypeptide of EQCDFKENGLVQRCTGTVTLDSAFNVSSLSC
11 kDa LGGRRFRRMVGLRKKFRKTRKRIQKLGRKIG
KTGRKVWKAWREYGQIPYPCRI
Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide porcellus KMKGDREDHVAVISFWEEESTSLEDAGAGA
1 precursor GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC
(Neutrophil C
defensin)
(GPNP)
(Corticostatic
peptide GP-
CS1) (CP-1)
Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide porcellus KMKGDREDHVAVISFWEEESTSLQDAGAGA
1B precursor GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC
(Neutrophil C
defensin) (CP-
1B) (GNCP)
Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDT
cationic peptide porcellus KMKGDREDHVAVISFWEEESTSLQDAGAGA
2 precursor GRRCICTTRTCRFPYRRLGTCLFQNRVYTFC
(CP-2) (GNCP) C
(GNCP-2)
Neutrophil Mesocricetus 33 VTCFCRRRGCASRERHIGYCRFGNTIYRLCC
defensin 1 auratus RR
(HANP-1)
Neutrophil Mesocricetus 31 CFCKRPVCDSGETQIGYCRLGNTFYRLCCR
defensin 2 auratus Q
(HANP-2)
Neutrophil Macaca 30 ACYCRIPACLAGERRYGTCFYMGRVWAFCC
defensin 2 mulatta
(RMAD-2)
Neutrophil Mesocricetus 33 VTCFCRRRGCASRERLIGYCRFGNTIYGLCC
defensin 3 auratus RR
(HANP-3)
Neutrophil Mesocricetus 33 VTCFCKRPVCDSGETQIGYCRLGNTFYRLCC
defensin 4 auratus RQ
(HANP-4)
Neutrophil Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAA
defensins 1, 3 mulatta QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
and 8 KNMACYCRIPACLAGERRYGTCFYLGRVWA
precursor FCC
(RMAD)
Neutrophil Macaca 94 MRTIAILAAILLFALLAQAKSLQETADDAATQE
defensins 4 mulatta QPGEDDQDLAVSFEENGLSTLRASGSQARR
and 5 TCRCRFGRCFRRESYSGSCNINGRIFSLCCR
precursor
(RMAD)
Neutrophil Macaca 94 MRTIAILAAILLFALLAQAKSLQETADEAATQE
defensins 6 mulatta QPGEDDQDLAVSFEENGLSTLRASGSQARR
and 7 TCRCRFGRCFRRESYSGSCNINGRISSLCCR
precursor
NK-lysin Sus scrofa 129 PGLAFSGLTPEHSALARAHPCDGEQFCQNLA
precursor PEDPQGDQLLQREELGLICESCRKIIQKLEDM
(NKL) VGPQPNEDTVTQAASRVCDKMKILRGVCKKI
(Fragment) MRTFLRRISKDILTGKKPQAICVDIKICKEKTG
LI
Nonhistone Oncorhynchus 69 PKRKSATKGDEPARRSARLSARPVPKPAAKP
chromosomal mykiss KKAAAPKKAVKGKKAAENGDAKAEAKVQAA
protein H6 GDGAGNAK
(Histone T)
[Contains:
Oncorhyncin
III]
Oligosacchar- Bos taurus 190 MSRRYTPLAWVLLALLGLGAAQDCGSIVSRG
ide-binding KWGALASKCSQRLRQPVRYVVVSHTAGSVC
protein NTPASCQRQAQNVQYYHVRERGWCDVGYN
FLIGEDGLVYEGRGWNTLGAHSGPTWNPIAI
GISFMGNYMHRVPPASALRAAQSLLACGAAR
GYLTPNYEVKGHRDVQQTLSPGDELYKIIQQ
WPHYRRV
Opistoporin 1 Opistophthalmus 44 GKVWDWIKSTAKKLWNSEPVKELKNTALNAA
carinatus KNLVAEKIGATPS
Opistoporin 2 Opistophthalmus 44 GKVWDWIKSTAKKLWNSEPVKELKNTALNAA
carinatus KNFVAEKIGATPS
Pandinin 1 Pandinus 44 GKVWDWIKSAAKKIWSSEPVSQLKGQVLNA
imperator AKNYVAEKIGATPT
Pandinin 2 Pandinus 24 FWGALAKGALKLIPSLFSSFSKKD
imperator
Parabutoporin Parabuthus 45 FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYA
schlechteri KGLLEGGSEEVPGQ
Penaeidin-1 Litopenaeus 50 YRGGYTGPIPRPPPIGRPPLRLVVCACYRLSV
(Pen-1) (P1) vannamei SDARNCCIKFGSCCHLVK
Penaeidin-2a Litopenaeus 72 MRLVVCLVFLASFALVCQGEAYRGGYTGPIP
precursor (Pen- vannamei RPPPIGRPPFRPVCNACYRLSVSDARNCCIK
2a) (Pen-2) FGSCCHLVKG
(P2)
Penaeidin-2b Litopenaeus 72 MRLVVCLVFLASFALVCQGEAYRGGYTGPIP
precursor (Pen- vannamei RPPPIGRPPLRPVCNACYRLSVSDARNCCIK
2b) FGSCCHLVKG
Penaeidin-2d Litopenaeus 72 MRLVVCLVFLASFALVCQGGAQRGGFTGPIP
precursor (Pen- setiferus RPPPHGRPPLGPICNACYRLSFSDVRICCNFL
2d) GKCCHLVKG
Penaeidin-3a Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3a) (P3-a) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3b Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPVP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3b) (P3-b) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3c Litopenaeus 81 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPFVRPVPGGPIGPYNGCPVSCRGiSFSQA
3c) (P3-c) RSCCSRLGRCCHVGKGYSG
Penaeidin-3d Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3d) RSCCSRLGRCCHVGKGYSG
Penaeidin-3e Litopenaeus 82 MRLVVCLVFLAPFALVCHGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ
3e) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3f Litopenaeus 82 MRLVACLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3f) RSCCSRLGRCCHVGKGYSG
Penaeidin-3g Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPISPYNGCPVSCRGISFSQ
3g) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3h Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA
3h) RSYCSRLGRCCHVGKGYSG
Penaeidin-3i Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGRPVSCRGISFSQ
3i) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3j Litopenaeus 81 MRLVVCLVFLASFALVCQGQVYKGGYTRPVP
precursor (Pen- vannamei RPPFVRPLPGGPIGPYNGCPVSCRGISFSQA
3j) RSCCSRLGRCCHVGKGYSG
Penaeidin-3k Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNACTLSCRGITTTQARSCCTR
3k) LGRCCHVAKGYSG
Penaeidin-3l Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNVCTLSCRGITTTQARSCCTR
3l) LGRCCHVAKGYSG
Penaeidin-3m Litopenaeus 75 MRLVVCLVFLASFALVCQGQGCKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNACTLSCRGITTTQARSCCTR
3m) LGRCCHVAKGYSG
Penaeidin-3n Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNACTLSCRGITTTQARSCSTR
3n) LGRCCHVAKGYSG
Penaeidin-4a Litopenaeus 67 MRLVVCLVFLASFALVCQGHSSGYTRPLPKP
precursor (Pen- vannamei SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4a) CHRG
Penaeidin-4c Litopenaeus 67 MRLVVCLVFLASFALVCQGYSSGYTRPLPKP
precursor (Pen- vannamei SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4c) CHRG
Penaeidin-4d Litopenaeus 67 MRLLVCLVFLASFAMVCQGHSSGYTRPLRKP
precursor (Pen- setiferus SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC
4d) CHLG
Phormicin Protophormia 94 MKFFMVFVVTFCLAVCFVSQSLAIPADAAND
precursor terraenovae AHFVDGVQALKEIEPELHGRYKRATCDLLSG
(Insect TGINHSACAAHCLLRGNRGGYCNGKGVCVC
defensins A RN
and B)
Phylloxin Phyllomedusa 64 MVFLKKSLLLVLFVGLVSLSICEENKREEHEEI
precursor bicolor EENKEKAEEKRGWMSKIASGIGTFLSGMQQ
G
Pleurocidin Pseudopleur- 25 GWGSFFKKAAHVGKHVGKAALHTYL
onectes
americanus
Pleurocidin 2 Pseudopleur- 68 MKFTATFLMMAIFVLMVEPGECGWGSFFKKA
precursor onectes AHVGKHVGKAALTHYLGDKQELNKRAVDED
americanus PNVIVFE
Pleurocidin Pseudopleur- 68 MKFTATFLMIAIFVLMVEPGECGWGSFFKKA
prepropoly- onectes AHVGKHVGKAALTHYLGDKQELNKRAVDED
peptide americanus PNVIVFE
Pleurocidin Pseudopleur- 68 MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly- onectes RHAAKHIGHAAVNHYLGEQQDLDKRAVDED
peptide americanus PNVIVFE
Pleurocidin Pseudopleur- 60 MKFTATFLMIAIFVLMVEPGECGWGSFFKKA
prepropoly- onectes AHVGKHVGKAALTHYLGDKQELNKRAVDE
peptide americanus
(Fragment)
Pleurocidin Pseudopleur- 60 MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly- onectes RHAAKHIGHAAVNHYLGEQQDLDKRAVDE
peptide americanus
(Fragment)
Pleurocidin-like Pseudopleur- 89 MKFTATFLLLFIFVLMVDLGEGRRKKKGSKRK
prepropoly- onectes GSKGKGSKGKGRWLERIGKAGGIIIGGALDH
peptide americanus LGQGQVQGPDYDYQEGEELNKRAVDE
(Fragment)
Pleurocidin-like Pseudopleur- 72 MKFTATFLLLFIFVLMVDLGEGRRKRKWLRRI
prepropoly- onectes GKGVKIIGGAALDHLGQGQVQGQDYDYQEG
peptide americanus QELNKRAVDE
(Fragment)
Pleurocidin-like Pseudopleur- 61 MKFTATFLVLSLVVLMAEPGECFLGALIKGAI
prepropoly- onectes HGGRFIHGMIQNHHGYDEQQELNKRAVDE
peptide americanus
(Fragment)
Polyphemusin I Limulus 18 RRWCFRVCYRGFCYRKCR
polyphemus
Polyphemusin Limulus 18 RRWCFRVCYKGFCYRKCR
II polyphemus
Ponericin G1 Pachycondyla 30 GWKDWAKKAGGWLKKKGPGMAKAALKAAM
goeldii Q
Ponericin G2 Pachycondyla 30 GWKDWLKKGKEWLKAKGPGIVKAALQAATQ
goeldii
Ponericin G3 Pachycondyla 30 GWKDWLNKGKEWLKKKGPGIMKAALKAATQ
goeldii
Ponericin G4 Pachycondyla 29 DFKDWMKTAGEWLKKKGPGILKAAMAAAT
goeldii
Ponericin G5 Pachycondyla 30 GLKDWVKIAGGWLKKKGPGILKAAMAAATQ
goeldii
Ponericin G6 Pachycondyla 18 GLVDVLGKVGGLIKKLLP
goeldii
Ponericin G7 Pachycondyla 19 GLVDVLGKVGGLIKKLLPG
goeldii
Ponericin L1 Pachycondyla 24 LLKELWTKMKGAGKAVLGKIKGLL
goeldii
Ponericin L2 Pachycondyla 24 LLKELWTKIKGAGKAVLGKIKGLL
goeldii
Ponericin W1 Pachycondyla 25 WLGSALKIGAKLLPSWGLFKKKKQ
goeldii
Ponericin W2 Pachycondyla 25 WLGSALKIGAKLLPSWGLFQKKKK
goeldii
Ponericin W3 Pachycondyla 26 GIWGTLAKIGIKAVPRVISMLKKKKQ
goeldii
Ponericin W4 Pachycondyla 26 GIWGTALKWGVKLLPKLVGMAQTKKQ
goeldii
Ponericin W5 Pachycondyla 24 FWGALIKGAAKLIPSWGLFKKKQ
goeldii
Ponericin W6 Pachycondyla 20 FIGTALGIASAIPAIVKLFK
goeldii
Preprodefensin Boophilus 74 MRGIYICLXFVLXCGLVSGLADVPAESEMAHL
microplus RVRRGFGCPFNQGACHRHCRSIRRRGGYCA
GLIKQTCTCYRN
preprodefensin Ixodes 76 MKVLAVSLAFLLIAGLISTSLAQNEEGGEKELV
ricinus RVRRGGYYCPFFQDKCHRHCRSFGRKAGY
CGGFLKKTCICVMK
Probable Riptortus 678 MRSPRVIHLACVIAYIVAVEAGDKPVYLPRPT
antibacterial clavatus PPRPIHPRLAREVGWELEGQGLSPLSEAELL
peptide PEVRERRSPVDKGGYLPRPTPPRPVYRSRR
polyprotein DASLESELSPLSVAEVLPEVRERRSPVDKGG
precursor YLPRPTPPRPVYRSRRDASLESELSPLSEAE
VLPEVRERRSPVDKGGYLPRPTPPRPVYRS
RRVASLESELSPLSEAEVLPEVRERRSPVDK
GGYLPRPTPPRPVYRSRRDASLESELSPLSE
EEVLPEVRERGSPVDKGGYLPRPTPPRPVY
RSRRDASLESELSPLSVAEDLPEVRERRSPV
DKGGYLPRPTPPRPVYRSRRDASLESELSPL
SEAEVLPEVRERRSPVDKGGYLPRPTPPRPV
YRSRRDASLESELSPLSEAEVLPEVRERRSP
VDKGGYLPRPTPPRPVYRSRRDASLESELSP
LSEAEVLPEVRERRSPVDKGGYLPRPTPPRP
VYRSRRDASLESELSPLSEAEVLPEVRERRS
PVDKGGYLPRPTPPRPVYRSRRDATLESELS
PSSEAEVLPEVRERRSPVDKGGYLPRPTPPR
PVYRSRRDASLESELSPLSEAEVLPEVRERR
SPVDKGGYLPRPTPPRPVYRSRRDASLESEL
SPLSEAEGLPEVRERRSPGGQGGYLPRPTP
RTPLCRSRRDANLDAEQSPVSEGWLPEVR
Probable Riptortus 150 MHIARFCLLSSMAVLALSAGYVSGAVIEIPDEI
antibacterial clavatus LDSARFISLYSDGLRQKRQLNLSGPGSEHAG
peptide TIRLDGQRNIFDNGRTRVDGTGSYQLDYARG
precursor MKPIHGAGLGAEVNHNIWRGRGGQSLDLYG
GATRQFNFGNRPNEWGAHGGIRYNF
Proenkephalin Bos taurus 263 MARFLGLCTWLLALGPGLLATVRAECSQDCA
A precursor TCSYRLARPTDLNPLACTLECEGKLPSLKTW
[Contains: ETCKELLQLTKLELPPDATSALSKQEESHLLA
Synenkephalin KKYGGFMKRYGGFMKKMDELYPLEVEEEAN
Met-enkephalin GGEVLGKRYGGFMKKDAEEDDGLGNSSNLL
(Opioid growth KELLGAGDQREGSLHQEGSDAEDVSKRYGG
factor) (OGF); FMRGLKRSPHLEDETKELQKRYGGFMRRVG
Met- RPEWWMDYQKRYGGFLKRFAEPLPSEEEG
enkephalin- ESYSKEVPEMEKRYGGFMRF
Arg-Gly-Leu;
Leu-
enkephalin;
Enkelytin; Met-
enkephalin-
Arg-Phe]
Prophenin-1 Sus scrofa 212 LLLLALVVPSASAQALSYREAVLRAVDRLNEQ
precursor (PF- SSEANLYRLLELDQPPKADEDPGTPKPVSFT
1) (C6) VKETVCPRPTRQPPELCDFKENGRVKQCVG
(Fragment) TVTLDQIKDPLDITCNEGVRRFPWWWPFLRR
PRLRRQAFPPPNVPGPRFPPPNFPGPRFPP
PNFPGPRFPPPNFPGPRFPPPNFPGPPFPPP
IFPGPWFPPPPPFRPPPFGPPRFPGRR
Prophenin-2 Sus scrofa 228 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PF- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
2) (PR-2) (C12) PPKADEDPGTPKPVSFTVKETVCPRPTRRPP
(Prophenin-1 ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
like) EGVRRFPWWWPFLRRPRLRRQAFPPPNVP
GPRFPPPNVPGPRFPPPNFPGPRFPPPNFP
GPRFPPPNFPGPPFPPPIFPGPWFPPPPPFR
PPPFGPPRFPGRR
Protegrin 1 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
1) (Neutrophil PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
peptide 1) ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
EVQGVRGGRLCYCRRRFCVCVGRG
Protegrin 2 Sus scrofa 147 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
2) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
EVQGVRGGRLCYCRRRFCICVG
Protegrin 3 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
3) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
EVQGVRGGGLCYCRRRFCVCVGRG
Protegrin 4 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PG- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ
4) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN
EVQGVRGGRLCYCRGWCFCVGRG
Protegrin 5 Sus scrofa 149 METQRASLCLGRWSLWLLLLGLVVPSASAQ
precursor (PG- ALSYREAVLRAVDRLNEQSSEANLYRLLELD
5) QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
PELCDFKENGRVKQCVGTVTLDQIKDPLDITC
NEVQGVRGGRLCYCRPRFCVCVGRG
Protegrin-1 Sus scrofa 19 RGGRLCYCRRRFCVCVGRX
Pseudin 1 Pseudis 24 GLNTLKKVFQGLHEAIKLINNHVQ
paradoxa
Pseudin 2 Pseudis 24 GLNALKKVFQGIHEAIKLINNHVQ
paradoxa
Pseudin 3 Pseudis 23 GINTLKKVIQGLHEVIKLVSNHE
paradoxa
Pseudin 4 Pseudis 23 GINTLKKVIQGLHEVIKLVSNHA
paradoxa
Putative Litopenaeus 188 MKGIKAVILCGLFTAVLAGKYRGFGQPLGGL
antimicrobial setiferus GVPGGGVGVGVGGGLGGGLGGGLGGGLG
peptide GGLGGGLGGLGGGLGGLGGGLGGGLGGGL
GGGLGGGLGGSHGTSDCRYWCKTPEGQAY
CCESAHEPETPVGTKPLDCPQVRPTCPRFH
GPPTTCSNDYKCAGLDKCCFDRCLGEHVCK
PPSFFGQQIFG
Putative Litopenaeus 123 MKGLGVILCCVLAVVPAHAGPGGFPGGVPG
antimicrobial setiferus RFPSATAPPATCRRWCKTPENQAYCCETIFE
peptide PEAPVGTKPLDCPQVRPTCPRFHGPPVTCS
SDYKCGGVDKCCFDRCLGEHVCKPPSFYSQ
FP
Putative Litopenaeus 141 MKGLGVILCCVLAVVPAHAGPGGFSGGVPG
antimicrobial setiferus GFPGGRPGGFPGGVPGGFPSATAPPATCRR
peptide WCKTPENQAYCCETIFEPEAPVGTKPLDCPQ
VRPTCPPTRFGGRPVTCSSDYKCGGLDKCC
FDRCLGEHVCKPPSFYSQFR
Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKILDCPQVRPTCP
RFHGPPTTCSNDYKCAGLDKCCFDRCLGEH
VCKPPSFFGSQVFG
Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKPLDCPQVRPTC
PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
HVCKPPSFFGSQVFG
Putative Litopenaeus 169 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide GLGVGGGLGVGGGLGVGGGLGTGTSDCRY
WCKTPEGQAYCCESAHEPETPVGTKILDCP
QVRPTCPRFHGPPTTCSNDYKCAGLDKCCF
DRCLGEHVCKPPSFFGSQVFG
Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL
antimicrobial vannamei GGPGGSVGVGGGFPGGGLGVGGGLGVGG
peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKPLDCPQVRPTC
PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
HVCKPPSFFGSQVFG
Putative Litopenaeus 151 MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide GLGTGTSDCRYWCKTPEGQAYCCESAHEPE
TPVGTKPLDCPQVRPTCPRFHGPPTTCSND
YKCAGLDKCCFDRCLGEHVCKPPSFFGSQV
FG
Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG
peptide GLGVGGGLGVGGGLGTGTSDYRYWCKTPE
GQAYCCESAHEPETPVGTKPLDCPQVRPTC
PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
HVCKPPSFFGSQVFG
Putative beta Mus 79 MKTFLFLFAVLFFLDPAKNAFFDEKCSRVNG
defensin musculus RCTASCLKNEELVALCQKNLKCCVTVQPCGK
SKSNQSDEGSGHMGTWG
Putative beta Mus 63 MPQTFFVFCFLFFVFLQLFPGTGEIAVCETCR
defensin musculus LGRGKCRRACIESEKIVGWCKLNFFCCRERI
Putative beta Mus 64 MRIFSLIVAGLVLLIQLYPAWGTLYRRFLCKK
defensin musculus MNGQCEAECFTFEQKIGTCQANFLCCRKRK
EH
Putative beta Mus 67 MRTLCSLLLICCLLFSYTTPAANSIIGVSEMER
defensin musculus CHKKGGYCYFYCFSSHKKIGSCFPEWPRCC
KNIK
Putative beta Mus 77 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ
defensin musculus LARCYKFGGFCYNSMCPPHTKFIGNCHPDHL
HCCINMKELEGST
Putative beta Mus 73 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ
defensin musculus LTRCYKFGGFCHYNICPGNSRFMSNCHPENL
RCGKNIKQF
Putative Mesobuthus 61 MTYAILIIVSLLLISDRISNVVDKYGSENPLDCN
potassium martensii EHCLKTKNQIGICHGANGNEKCSCMES
channel
blocker TXKs2
PYLa/PGLa Xenopus 64 MYKQIFLCLIIAALCATIMAEASAFADADEDDD
precursor laevis KRYVRGMASKAGAIAGKIAKVALKALGRRDS
Pyrrhocoricin Pyrrhocoris 20 VDKGSYLPRPTPPRPIYNRN
apterus
Ranalexin Rana 66 MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor catesbeiana RDNPDERDVEVEKRFLGGLIKIVPAMICAVTK
KC
Ranalexin-1CA Rana 20 FLGGLMKAFPALICAVTKKC
clamitans
Ranalexin-1CB Rana 20 FLGGLMKAFPAIICAVTKKC
clamitans
Ranatuerin-1C Rana 25 SMLSVLKNLGKVGLGLVACKINKQG
clamitans
RANATUERIN- Rana 28 GLLDTIKGVAKTVAASMLDKLKCKISGC
2B berlandieri
Ranatuerin- Rana 31 GLFLDTLKGAAKDVAGKLLEGLKCKIAGGKP
2CA clamitans
Ranatuerin- Rana 27 GLFLDTLKGLAGKLLQGLKGIKAGCKP
2CB clamitans
RANATUERIN- Rana 32 GILSSIKGVAKGVAKNVAAQLLDTLKCKITGC
2LB luteiventris
RANATUERIN- Rana pipiens 27 LMDTVKNVAKNLAGHMLDKLKCKITGC
2P
RANATUREIN- Rana 32 GILDSFKGVAKGVAKDLAGKLLDKLKGKITGC
2LA luteiventris
Rhinocerosin Oryctes 142 MMKLYIVFGFIAFSAAYVVPEGYYEPEYYPAD
precursor rhinoceros GYESERVARASPAELIFDEDLADEPEVEEPQ
YYIRTRRSLQPGAPNFPMPGSQLPTSITSNIE
KQGPNTAATINAQHKTDRYDVGATWSKVIRG
PGRSKPNWSIGGTYRW
Royalism Apis mellifera 95 MKIYFIVGLLFMAMVAIMAAPVEDEFEPLEHF
precursor ENEERADRHRRVTGDLLSFKGQVNDSAGAA
(Defensin) NGLSLGKAGGHGEKVGGIGRKTSFKDLWDK
RFG
Rugosin A Rana rugosa 33 GLLNTFKDWAISIAKGAGKGVLTTLSGKLDKS
C
Rugosin B Rana rugosa 33 SLFSLIKAGAKFLGKNLLKQGAQYAACKVSKE
C
Rugosin C Rana rugosa 37 GILDSFKQFAKGVGKDLIKGAAQGVLSTMSC
KLAKTC
Sapecin B Sarcophaga 88 MKFLTSLLLLFVVVMVSAVNLSMAKESANQL
precursor peregrina TERLQELDGAAIQEPAELNRHKRLTCEIDRSL
CLLHCRLKGYLRAYCSQQKVCRCVQ
Sapecin C Sarcophaga 40 ATCDLLSGIGVQHSACALHCVFRGNRGGYCT
peregrina GKGICVCRN
Sapecin Sarcophaga 94 MKSFIVLAVTLCLAAFFMGQSVASPAAAAEES
precursor peregrina KFVDGLHALKTIEPELHGRYKRATCDLLSGTG
INHSACAAHCLLRGNRGGYCNGKAVCVCRN
Sarcotoxin IA Sarcophaga 63 MNFQNIFIFVALILAVFAGQSQAGWLKKIGKKI
precursor peregrina ERVGQHTRDATIQGLGIAQQAANVAATARG
Sarcotoxin IB Sarcophaga 63 MNENKVFIEVALILAVFAGQSQAGWLKKIGKKI
precursor peregrina ERVGQHTRDATIQVIGVAQQAANVAATARG
Sarcotoxin IC Sarcophaga 39 GWLRKIGKKIERVGQHTRDATIQVLGIAQQAA
peregrina NVAATAR
Sarcotoxin ID Sarcophaga 40 GWIRDFGKRIERVGQHTRDATIQTIAVAQQAA
peregrina NVAATLKG
Sarcotoxin II-1 Sarcophaga 265 MKSFVLFAACMAIIALGSLAHAYPQKLPVPIPP
precursor peregrina PSNPPVAVLQNSVATNSKGGQDVSVKLSAT
NLGNNHVQPIAEVFAEGNTKGGNVLRGATV
GVQGHGLGASVTKTQTDTKIKGLDFQPQLSS
STLALQGDRLGASISRDVNRGVSDTFTKSVS
ANVFRNDNHNLDATVFRSDVRQNNGFNFQK
TGGMLDYSHANGHGLNAGLTHFSGIGNQAN
VGGSSTLFKSNDGSLSLKANAGGSQWLSGP
FSNQRDYNVGLSLTHHGCGG
Sarcotoxin II-2 Sarcophaga 294 MKSFVFFAACFAIVALNSLAHAYPQKLPVPIP
precursor peregrina PPTNPPVAAFHNSVATNSKGGQDVSVKLAAT
NLGNKHVQPIAEVFAKGNTQGGNVLRGATV
GVQGHGLGASVTKTQDGIAESFRKQAEANL
RLGDSASLIGKVSQTDTKIKGIDFKPQLSSSSL
ALQGDRLGASISRDVNRGVSDTLTKSISANVF
RNDNHNLDASVFRSDVRQNNGFNFQKTGG
MLDYSHANGHGLNAGLTRFSGIGNQANVGG
YSTLFRSNDGLTSLKANAGGSQWLSGPFAN
QRDYSFGLGLSHNAWRG
Sarcotoxin II-3 Sarcophaga 294 MKSFVLFAACMAIVALSSLAHAYPQKLPVPIP
precursor peregrina PPTNPPVAAFHNSVATNSKGGQDVSVKLXAT
NLGNKHVQPIAEVFAEGNTKGGNVIRGATVG
VQGHGLGASVTKSGNGIAESFRKQAEANLRL
GDSASLIGKVSQTDTKIKGIDFKPQLSSSSLAL
QGDRLGASISRDVNRGVSDTLTKSISANVFR
NDNHNLDASVFRSDVRQNNGFNFQKTGGML
DYSHANGHGLNAGLTRFSGIGNQANVGGYS
TLFRSNDGLTSLKANAGGSQWLSGPFANQR
DYSFGLGLSHNAWRG
Sarcotoxin IIA Sarcophaga 294 MKSFVFFAACMAIIALSSLVQAYPQKLPVPIPP
precursor peregrina PTNPPVAAFHNSVATNSKGGQDVSVKLAATN
LGNKHVQPIAEVFAEGNTKGGNVLRGATVGV
QGHGLGASVTKSQDGIAESFRKQAEANLRLG
DSASLIGKVSQTDTKIKGIDFKPQLSSSSLALQ
GDRLGASISRDVNRGVSDTLTKSVSANLFRN
DNHNLDASVFRSDVRQNNGFNFQKTGGMLD
YSHANGHGLNAGLTRFSGIGNQATVGGYSTL
FRSNDGLTSLKANAGGSQWLSGPFANQRDY
SFGLGLSHNAWRG
Scorpine Pandinus 94 MNSKLTALIFLGLIAIAYCGWINEEKIQKKIDER
precursor imperator MGNTVLGGMAKAIVHKMAKNEFQCMANMD
MLGNCEKHCQTSGEKGYCHGTKCKCGTPLS
Y
Secretogranin I Bos taurus 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEE
precursor (Sgl) VVTHCIIEVLSNALLKSSAPPITPECRQVLKKN
(Chromogranin GKELKNEEKSENENTRFEVRLLRDPADTSEA
B) (CgB) PGLSSREDSGEGDAQVPTVADTESGGHSRE
[Contains: RAGEPPGSQVAKEAKTRYSKSEGQNREEEM
GAWK peptide; VKYQKRERGEVGSEERLSEGPGKAQTAFLN
Secretolytin] QRNQTPAKKEELVSRYDTQSARGLEKSHSR
ERSSQESGEETKSQENWPQELQRHPEGQE
APGESEEDASPEVDKRHSRPRHHHGRSRPD
RSSQEGNPPLEEESHVGTGNSDEEKARHPA
HFRALEEGAEYGEEVRRHSAAQAPGDLQGA
RFGGRGRGEHQALRRPSEESLEQENKRHGL
SPDLNMAQGYSEESEEERGPAPGPSYRARG
GEAAAYSTLGQTDEKRFLGETHHRVQESQR
DKARRRLPGELRNYLDYGEEKGEEAARGKW
QPQGDPRDADENREEARLRGKQYAPHHITE
KRLGELLNPFYDPSQWKSSRFERKDPMDDS
FLEGEEENGLTLNEKNFFPEYNYDWWEKKP
FEEDVNWGYEKRNPVPKLDLKRQYDRVAEL
DQLLHYRKKSAEFPDFYDSEEQMSPQHTAE
NEEEKAGQGVLTEEEEKELENLAAMDLELQK
IAEKFSGTRRG
Similar to Mus 93 MKKLVLLSALVLLAYQVQTDPIQNTDEETNTE
cryptdin-4 musculus EQPGEEDQAVSVSFGGQEGSALHEKLSRDLI
CLCRKRRCNRGELFYGTCAGPFLRCCRRRR
Similar to Mus 93 MKTLVLLSALILLAYQVQTDPIQNTDEETNTEE
cryptdin-4 musculus QPGEDDQAVSVSFGGQEGSALHEKLSRDLIC
LCRNRRCNRGELFYGTCAGPFLRCCRRRR
Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4 musculus EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI
CYCRKGGCNRGEQVYGTCSGRLLFCCRRR
HRH
Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4 musculus EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI
CYCRKGGCNRGEQVYGTCSGRLLLCCRRR
HRH
Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTE
cryptdin-4 musculus EQPGEEDQAVSVSFGDPEGSALHEKSSRDLI
CYCRKGGCNRGEQVYGTCSGRLLFCCRRR
HRH
Single WAP Mus 80 MKLLGLSLLAVTILLCCNMARPEIKKKNVFSK
motif protein 1 musculus PGYCPEYRVPCPFVLIPKCRRDKGCKDALKC
precursor CFFYCQMRCVDPWESPE
(Elafin-like
protein I)
Single WAP Mus 85 MWPNSILVLMTLLISSTLVTGGGVKGEEKRV
motif protein 2 musculus CPPDYVRCIRQDDPQCYSDNDCGDQEICCF
precursor WQCGFKCVLPVKDNSEEQIPQSKV
(Elafin-like
protein II)
Spingerin Pseudacan- 25 HVDKKVADKVLLLKQLRIMRLLTRL
thotermes
spiniger
Styelin A Styela clava 20 GXFGKAFXSVSNFAKKHKTA
(Fragment)
Styelin B Styela clava 20 GXFGPAFHSVSNFAKKHKTA
(Fragment)
Styelin C Styela clava 80 MQMKATILIVLVALFMIQQSEAGWFGKAFRSV
precursor SNFYKKHKTYIHAGLSAATLLGDMTDEEFQE
FMQDIEQAREEELLSRQ
Styelin D Styela clava 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSV
precursor GKFYYKHKYYIKAAWQIGKHALGDMTDEEFQ
DFMKEVEQAREEELQSRQ
Styelin E Styela clava 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSV
precursor GKFYYKHKYYIKAAWKIGRHALGDMTDEEFQ
DFMKEVEQAREEELQSRQ
T22H6.7 Caenorhabditis 195 MFRKLIIATFVLSLCDLANSVTICSSSSLLSTFT
protein (ABF-6) elegans DPLCTSWCKVRFCSSGSCRSVMSGSDPTCE
CESCGFGSWFGSSSDSNSNQPVSGQYYAG
GSGGEMATPNYGNNNGYNNGYNNGNNMRY
NDNNGYNTNNGYRGQPTPGYGNSNSNFNS
NQQYSYQQYYNNRNNQYGNSGYGNAGQAG
QTGYPSGYQNLKKKR
tachycitin Tachypleus 98 MASSFMFAVVVLFISLAANVESYLAFRCGRY
precursor tridentatus SPCLDDGPNVNLYSCCSFYNCHKCLARLEN
CPKGLHYNAYLKVCDWPSKAGCTSVNKECH
LWKTGRK
Tachyplesin I Tachypleus 77 MKKLVIALCLMMVLAVMVEEAEAKWCFRVCY
precursor tridentatus RGICYRRCRGKRNEVRQYRDRGYDVRAIPE
ETFFTRQDEDEDDDEE
Tachyplesin II Tachypleus 77 MKKLVIALCLMMVLAVMVEEAEARWCFRVCY
precursor tridentatus RGICYRKCRGKRNEVRQYRDRGYDVRAIPD
ETFFTRQDEDEDDDEE
Tachystatin A2 Tachypleus 67 MKLQNTLILIGCLFLMGAMIGDAYSRCQLQGF
precursor tridentatus NCVVRSYGLPTIPCCRGLTCRSYFPGSTYGR
CQRY
Temporin A Rana 13 FLPLIGRVLSGIL
temporaria
Temporin B Rana 61 MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor temporaria RDEPDERDVQVEKRLLPIVGNLLKSLLGK
Temporin C Rana 13 LLPILGNLLNGLL
temporaria
Temporin D Rana 13 LLPIVGNLLNSLL
temporaria
Temporin E Rana 13 VLPIIGNLLNSLL
temporaria
Temporin F Rana 13 FLPLIGKVLSGIL
temporaria
Temporin G Rana 61 MFTLKKSLLLLFFLGTINLSLCEEERDADEER
precursor temporaria RDDLEERDVEVEKRFFPVIGRILNGILGK
Temporin H Rana 58 MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor temporaria RDEPDERDVQVEKRLSPNLLKSLLGK
Temporin K Rana 10 LLPNLLKSLL
temporaria
Temporin L Rana 13 FVQWFSKFLGRIL
temporaria
Temporin-1CA Rana 13 ELPELAKILTGVL
clamitans
Temporin-1CB Rana 13 FLPLFASLIGKLL
clamitans
Temporin-1CC Rana 13 FLPFLASLLTKVL
clamitans
Temporin-1CD Rana 13 FLPFLASLLSKVL
clamitans
Temporin-1CE Rana 13 FLPFLATLLSKVL
clamitans
Temporin-1Ja Rana 13 ILPLVGNLLNDLL
japonica
Temporin-1LA Rana 13 VLPLISMALGKLL
luteiventris
Temporin-1LB Rana 14 NFLGTLINLAKKIM
luteiventris
Temporin-1LC Rana 14 FLPILINLIHKGLL
luteiventris
Temporin-1P Rana pipiens 13 FLPIVGKLLSGLL
Tenecin 1 Tenebrio 84 MKLTIFALVACFFILQIAAFPLEEAATAEEIEQG
precursor molitor EHIRVKRVTCDILSVEAKGVKLNDAACAAHCL
FRGRSGGYCNGKRVCVCR
Tenecin 3 Tenebrio 96 MKTFVICLILVVAVSAAPDHHDGHLGGHQTG
precursor molitor HQGGQQGGHLGGQQGGHLGGHQGGQPGG
HLGGHQGGIGGTGGQQHGQHGPGTGAGHQ
GGYKTHGH
Termicin Pseudacan- 36 ACNFQSCWATCQAQHSIYFRRAFCDRSQCK
thotermes CVFVRG
spiniger
Testis defensin Mus 41 MKTLVLLSALFLLAFQVQADPIQNTDEETNTE
(Fragment) musculus VQPQEEDQA
Testis defensin Mus 40 MKTLVLLSPSSCWPSRSRLILSKTQMKRLKL
(Fragment) musculus RSSQRKRTR
Testis-specific Mus 83 MRLALLLLAILVATELVVSGKNPILQCMGNRG
beta-defensin- musculus FCRSSCKKSEQAYFYCRTFQMCCLQSYVRIS
like protein LTGVDDNTNWSYEKHWPRIP
Thanatin Podisus 21 GSKKPVPIIYCNRRTGKCQRM
maculiventris
Theta Defensin Macaca 18 GFCRCLCRRGVCRCICTR
1 mulatta
theta defensin Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA
1a precursor mulatta AQQQPGTDDQGMAHSFTWPENAALPLSESA
KGLRCICTRGFCRLL
theta defensin Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA
1b precursor mulatta AQQQPGADDQGMAHSFTRPENAALPLSESA
RGLRCLCRRGVCQLL
theta defensin- Macaca 18 RCICTRGFCRCLCRRGVC
1 mulatta
Tigerinin-1 Hoplobatrachus 11 FCTMIPIPRCY
tigerinus
Tigerinin-2 Hoplobatrachus 12 RVCFAIPLPICH
tigerinus
Tigerinin-3 Hoplobatrachus 12 RVCYAIPLPICY
tigerinus
Tigerinin-4 Hoplobatrachus 11 RVCYAIPLPIC
tigerinus
tracheal Bos taurus 64 MRLHHLLLALLFLVLSASSGFTQGVGNPVSC
antimicrobial VRNKGICVPIRCPGNMKQIGTCVGRAVKCCR
peptide KK
Tracheal Bos taurus 64 MRLHHLLLALLFLVLSAWSGFTQGVGNPVSC
antimicrobial VRNKGICVPIRCPGSMKQIGTCVGRAVKCCR
peptide KK
precursor
(TAP)
Xenopsin Xenopus 81 MYKGIFLCVLLAVICANSLATPSSDADEDNDE
precursor laevis VERYVRGWASKIGQTLGKIAKVGLKELIQPKR
[Contains: EAMLRSAEAQGKRPWIL
Xenopsin
precursor
fragment
(XPF);
Xenopsin]
Plant Antimicrobial Peptides
Protein Name Organism Name Length Sequence
22K Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGR
antifungal QLNRGESWRITAPAGTTAARIWAR
protein TGCQFDASGRGSCRTGDCGGVVQC
TGYGRAPNTLAEYALKQFNNLDFF
DISLIDGFNVPMSFLPDGGSGCSR
GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANNCHPTN
YSRYFKGQCPDAYSYPKDDATSTF
TCPAGTNYKVVFCP
AC- Amaranthus 29 VGECVRGRCPSGMCCSQFGYCGKG
AMP1 = caudatus PKYCG
ANTIMICROBIAL
peptide
Alpha- Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGR
amylase/ QLNRGESWRITAPAGTTAARIWAR
trypsin TGCQFDASGRGSCRTGDCGGVVQC
inhibitor TGYGRAPNTLAEYALKQFNNLDFF
(Antifungal DISILDGFNVPYSFLPDGGSGCSR
protein) GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANNCHPTN
YSRYFKGQCPDAYSYPKDDATSTF
TCPAGTNYKVVFCP
Alpha- Basella alba 20 GADFQECMKEHSQKQHQHQG
basrubrin
(Fragment)
antifungal Linum 37 ARFDIQNKCPYTVWAASVPVGGGR
25K protein usitatissimum QLNSGQTWXIDAP
antifungal Diospyros 30 ATFDIQNKXTYTVWAAAWAPSYPG
27K protein texana GXKQLD
antifungal 2S Raphanus 20 PQGPQQRPPLLQQCCNNLLQ
storage sativus
albumin large
chain
antifungal 2S Raphanus 30 PAGPFRIPRCRREFQQAQHLRACQ
storage sativus QWLHRQ
albumin small
chain
Antifungal Phytolacca 38 AGCIKNGGRCNASAGPPYCCSSYC
Peptide americana FQIAGQSYGVCKNR
Antifungal Eucommia 41 QTCASRCPRPCNAGLCCSIYGYCG
peptide 1 ulmoides SGNAYCGAGNCRCQCRG
(EAFP1)
Antifungal Eucommia 41 QTCASRCPRPCNAGLCCSIYGYCG
peptide 2 ulmoides SGAAYCGAGNCRCQCRG
(EAFP2)
Antifungal Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI
protein elata PAFASDRLNSDHQLDTGGSLAQGG
YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS
RAIWASNTNRQKGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT
VIPHSNGTAAASGAAQNKVNELYI
SMY
Antifungal Gastrodia 169 MASPASSAVIFLFAVAALMSLLAM
protein elata PALAASQLNAGQTLGTGQSLAQGP
DQFVIQNDCNLVLYDSNRVVWASG
TNGKASGCVLRMQRDGNLVIYSGS
RVIWASNTNRRDDNYYLLLQRDRN
VVIYDSSNNAIWATGTNVGNAAIT
VIPHSNGTAAASGAAQNKVNEYLR
P
Antifungal Ipomoea nil 92 MKFCTMFLVVLALASLLLTPSTIM
protein AQQCGSQARGRLCGNGLCCSQWGY
CGSTAAYCGAGCQSQCKSTAASAT
DTTTTANQSTAKSDPAGGAN
Antifungal Capsicum 85 MKFQVVILVLFALLLTRTSAQNCG
protein annuum RQAGRRVCANRLCCSQFGFCGTTR
EYCGAGCQSNCRRYATDTTGEGEN
VNNDEHKNNGGPN
Antifungal Ipomoea nil 91 MKYCTMFIVLLGLGSLLLTPTTIM
protein AQQCGRQASGRLCGNGLCCSQWGY
CGSTAAYCGAGCQSQCKSTAASST
TTTTANQSTAKSDPAGGAN
antifungal Sinapis alba 25 QKLCERPSGTWSGVCGNNNACKNQ
protein 1 C
antifungal Brassica 30 QKLCERPSGTWSGVCGNNNACKNQ
protein 1 napus CINLEK
antifungal Arabidopsis 27 QKLCERPSGTWSGVCGNSNACKNQ
protein 1 thaliana CIN
Antifungal Raphanus 51 XKLCERPSGTWSGVCGNNNACKNQ
Protein 1 sativus CINLEKARHGSCNYVFPAHKCICY
FPC
Antifungal Malva 15 VAGPFRIPPLRREFQ
protein 1 parviflora
large
subunit
(CW-1)
(Fragment)
Anti-fungal Phytolacca 65 MAKVSSAYLKFALVMILLLSVISA
protein 1 americana VMSAGCIKNGGRCNASAGPPYCCS
precursor SYCFQIAGQSYGVCKNR
(PAFP-S)
Antifungal Malva 16 PAGPFRIPPRXRXEFQ
protein 1 parviflora
small
subunit
(CW-1)
(Fragment)
antifungal Sinapis alba 26 QKLCQRPSGTWSGVCGNNNACRNQ
protein 2 CI
Antifungal Malva 20 PEDPQRRYQEXQREXRXQQE
protein 2 parviflora
large
subunit
(CW-2)
(Fragment)
Antifungal Malva 15 PEDPQRRYQEEQRRE
protein 3 parviflora
(CW-3)
(Fragment)
Antifungal Malva 37 DRQIDMEEQQLEKLNKQDRXPGLR
protein 4 parviflora YAAKQQMXTXRMG
(CW-4)
(Fragment)
Antifungal Malva 38 ITCGQVTSQVAGCLSYLQRGGAPA
protein 5 parviflora PXXXXGIRNLXXMA
(CW-5)
(Fragment)
Antifungal Beta vulgaris 46 AICKKPSKFFKGACGRDADCEKAC
protein AX1 DQENWPGGVCVPFLRCECQRSC
Antifungal Beta vulgaris 46 ATCRKPSMYFSGACFSDTNCQKAC
protein AX2 NREDWPNGKCLVGFKCECQRPC
Antifungal Gastrodia 129 SDRLNSGHQLDTGGSLAEGGYLFI
protein elata IQNDCNLVLYDNNRAVWASGTNGK
GAFP-1 ASGCVLKMQNDGNLVIYSGSRAIW
(Fragment) ASNTNRQNGNYYLILQRDRNVVIY
DNSNNAIWATHTNVGNAEITVIPH
SNGTAAASG
Antifungal Medicago 72 MEKKSLAGLCFLFLVLFVAQEIVV
protein sativa TEARTCENLADKYRGPCFSGCDTH
precursor CTTKENAVSGRCRDDFRCWCTKRC
Antifungal Gastrodia 178 MLEWGDGVFCGGCVGYLRGDSVEC
protein elata GNCSDRLNSGHQLDTGGSLAQGGY
precursor LFIIQNDCNLVLYDNNRAVWASGT
NGKASGCVLKMQNDGNLVIYSGSR
AIWASNTNRQNGNYYLILQRDRNV
VIYDNSNNAIWATHTNVGNAEITA
IPHSNGTAAASGAAQNKVNELYIS
MYSRSKRIAG
Antifungal Hordeum 44 ATITWNRCSYTVWPGALPGGGVRL
protein R vulgare DPGQRWALNMPAGTAGAAV
(Fragment)
Antifungal Hordeum 37 ATFTVINKCQYTVWAAAVPAGGGQ
protein S vulgare KLDAGQTWSIXXP
(Fragment)
Antifungal Arabidopsis 80 MAKSATIITFLFAALVLFAAFEAP
protein-like thaliana TMVEAQKLCEKPSGTWSGVCGNSN
ACKNQCINLEGAKHGSCNYVFPAH
KCICYVPC
Antimicrobial Pisum 60 ALSFLFLFLFVAQEIVVTEANTCE
detensin sativum HLADTYRGVCFTDASCDDHCKNKA
peptide HLISGTCHNFKC
DRR230-c
(Fragment)
Antimicrobial Macadamia 76 SAFTVWSGPGCNNRAERYSKCGCS
Peptide 1 integrifolia AIHQKGGYDFSYTGQTAALYNQAG
CSGVAHTRFGSSARACNPFGWKSI
FIQC
Antimicrobial Mesembryan 64 MAKVSSSLLKFAIVLILVLSMSAI
peptide 1 themum ISAKCIKNGKGCREDQGPPFCCSG
precursor crystallinum FCYRQVGWARGYCKNR
Antimicrobial Macadamia 102 MASTKLFFSVITVMMLIAMASEMV
peptide 1 integrifolia NGSAFTVWSGPGCNNRAERYSKCG
precursor CSAIHQKGGYDFSYTGQTAALYNQ
(AMP1) AGCSGVAHTRFGSSARACNPFGWK
SIFIQC
Antimicrobial Mirabilis 61 LPVAFLKFAIVLILFIAMSAMIEA
peptide 1 jalapa QCIGNGGRCNENVGPPYCCSGFCL
precursor RQPGQGYGYCKNR
(AMP1)
(MJ-AMP1)
(Fragment)
Antimicrobial Amaranthus 30 VGECVRGRCPSGMCCSQFGYCGKG
Peptide 2 caudatus PKYCGR
Antimicrobial Mirabilis 63 MAKVPIAFLKFVIVLILFIAMSGM
peptide 2 jalapa IEACIGNGGRCNENVGPPYCCSGF
precursor CLRQPNQGYGVCRNR
(AMP2)
(MJ-AMP2)
Antimicrobial Spinacia 22 XTCESPSHKFKGPCATNRNCES
peptide D1 oleracea
(So-D1)
(Defensin D1)
(Fragment)
Antimicrobial Spinacia 52 GIFSSRKCKTPSKTFKGICTRDSN
peptide D2 oleracea CDTSCRYEGYPAGDCKGIRRRCMC
(So-D2) SKPC
(Defensin D2)
(Fragment)
Antimicrobial Spinacia 25 GIFSSRKCKTVSKTFRGICTRNAN
peptide D3 oleracea C
(So-D3)
(Defensin D3)
(Fragment)
Antimicrobial Spinacia 23 MFFSSKKCKTVSKTFRGPCVRNA
peptide D4 oleracea
(So-D4)
(Defensin D4)
(Fragment)
Antimicrobial Spinacia 24 MFFSSKKCKTVXKTFRGPCVRNAN
peptide D5 oleracea
(So-D5)
(Defensin D5)
(Fragment)
Antimicrobial Spinacia 24 GIFSNMYXRTPAGYFRGPXGYXXN
peptide D6 oleracea
(So-D6)
(Defensin D6)
(Fragment)
Antimicrobial Spinacia 38 GIFSSRKCKTPSKTFKGYCTRDSN
peptide D7 oleracea CDTSCRYEGYPAGD
(So-D7)
(Defensin D7)
(Fragment)
Antimicrobial Zea mays 33 RSGRGECRRQCLRRHEGQPWETQE
peptide MBP-1 CMRRCRRRG
Antimicrobial Capsella 120 MASKTLILLGLFAILLVVSEVSAA
peptide shep- bursa- RESGMVKPESEETVQPEGYGGHGG
GRP pastoris HGGHGGHGGHGGHGHGGGGHGLDG
YHGGHGGHGGGYNGGGGHGGHGGG
YNGGGHHGGGGHGLNEPVQTQPGV
Antimicrobial Impatiens 333 MVQKGWFGVLLILFICSTLTSADS
peptides balsamina KPNPTKEEEPAKKPDEVSVKSGGP
precursor EVSEDQYRHRCCAWGPGRKYCKRW
(IB-AMP) CANAEEAAAAIPEASEELAQEEAP
[Contains: VYSEDQWGRRCCGWGPGRRYCVRW
Basic peptide CQNAEEAAAAIPEATEKAQEAPVY
AMP3 (IB- SEDQWGRRCCGWGPGRRYCVRWCQ
AMP3); Basic NAEEAAAAVAIPEASEKAQEGPVY
peptide AMP1- SEDQWGRRCCGWGPGRRYCVRWCS
1 (IB-AMP1- NAADEVATPEDVEPGQYGRRCCNW
1); Basic GPGRRYCKRWCHNAAEEATLKAFE
peptide AMP1- EEAAREQPVYSEDQWGRRCCGWGP
2 (IB-AMP1- GRRYCRRWCQSAEEAAAFQAGEVT
2); Basic ASLMLIMFKACPCMGPVPSV
peptide AMP1-
3 (IB-AMP1-
3); Basic
peptide A
Antimicrobial Allium cepa 132 MVRVVSLLAASTFILLIMIISSPY
protein Ace- ANSQNICPRVNRIVTPCVAYGLGR
AMP1 APIAPCCRALNDLRFVNTRNLRRA
precursor ACRCLVGVVNRNPGLRRNPRFQNI
PRDCRNTFVRPFWWRPRIQCGRIN
LTDKLIYLDAEE
Antimicrobial Ipomoea nil 41 QQCGRQASGRLCGNRLCCSQWGYC
protein PN- GSTASYCGAGCQSQCRS
AMP (PN-
AMP1/PN-
AMP2)
antimicrobial Amaranthus 86 MVNMKCVALIVIVMMAFMMVDPSM
protein hypochondriacus GVGECVRGRCPSGMCCSQFGYCGK
precursor GPKYCGRASTTVDHQADVAATKTA
KNPTDAKLAGAGSP
Antimicrobial Phytolacca 37 ACIKNGGRCVASGGPPYCCSNYCL
seed protein americana QIAGQSYGVCKKH
(Fragment)
avematin Avena sativa 26 TTITVVNKCSYTVWPGALPGGGVV
LD
Basal layer Zea mays 93 MAKFFNYTIIQGLLMLSMVLLASC
antifungal AIHAHIISGETEEVSNTGSPTVMV
peptide TMGANRKIIEDNKNLLCYLRALEY
precursor CCARTRQCYDDIKKCLEHCRG
Basal layer Zea mays 96 MVKILDHISIRGFFLLFMVLVASF
antifungal VGHAQIIRGETKEDNDTKSMTMTT
peptide MRPGSYVTSMDEKSSLCFEDIKTL
precursor WYICRTTYHLYRTLKDCLSHCNSM
Basal layer Zea mays 95 MVKSLDHITIRGLFLLFMFLVASF
antifungal VGHAQIIRGETKENKDTNSMTMTT
peptide RPGSYVISMDEKSSLCFLDPRTLW
precursor YICKITYRLFRTLKDCLEFCHSI
Basal layer Zea mays 73 MVLLASCVIHAHIISGEIEDVSNT
antifungal RSPTMMGANRKIIGDNKNLLCYLK
peptide ALEYCCERTKQCYDDIKKCLEHCH
precursor S
Beta-basrubin Basella alba 16 KIMAKPSKFYEQLRGR
(Fragment)
CBP20 Nicotiana 208 GKLSTLLLVLILYFIAAGANAQQC
(Fragment) tabacum GRQRGGALCSGNLCCSQFGWCGST
PEYCSPSQGCQSQCSGGGGGGGGG
GGGGAQNVRATYHIYNPQNVGWDL
YAVSAYCSTWDGNKPLAWRRKYGW
TAFCGPVGPRGRDSCGKCLRVTNT
GTGAQTTVRIVDQCSNGGLDLDVN
VFRQLDTDGRGNQRGHLIVNYEFV
NCGDNMNVLLSPVDKE
CBP20 Nicotiana 211 MGKLSTLLFALVLYVIAAGANAQQ
preproprotein tabacum CGRQRGGALCSGNLCCIQFGWCGS
TQEYCSPSQGCQSQCSGGGGGGGG
GGGGGGAAQNVRATYHIYNPQNVG
WDLYAVSAYCSTWDGNKPLAWRRK
YGWTAFCGPVGPRGRDSCGKCLRV
TNTGTGAQTTVRIVDQCSNGGLDL
DVNVFRQLDTDGRGNQRGHLIVNY
EFVNCGDNMNVLVSPVDKE
chitinase (EC Nicotiana 378 MANSVTLFSIIFSCFLLRQLVCTN
3.2.1.14)/ tabacum SQNVIKGGYWFKNSGLALNNIDST
lysozyme (EC LFTHLFCAFADLNPQSNQLIISPE
3.2.1.17) PZ NQDSFSQFTSTVQRKNPSVKTFLS
precursor, IAGGRADTTAYGIMARQPNSRKSF
pathogenesis- IDSSIRLARQFGFHGLDLDWEYPL
related SATDMTNLGILLNEWRTAINMEAR
NSGRAALLLTAAVSYSPRVNGLNY
PVESVARNLNWINLMAYDFYGPNW
SPSQTNSHAQLFDPVNHISGSDGI
NAWIQAGVPTKKLVLGIPFYGYAW
RLVNPNIHDLRAPAAGKSNVGAVD
DGSMTYNRIRDYIVQSRATTVYNA
TIVGDYCYSGSNWISYDDTQSVRN
KVNYVKGRGLLGYFAWHVAGDQNW
GLSRTASQTWGVSSQEMK
chitinase (EC Zea mays 280 MANAPRILALGLLALLCAAAGPAA
3.2.1.14) A AQNCGCQPNFCCSKFGYCGTTDAY
CGDGCQSGPCRSGGGGGGGGGGGG
GGSGGANVANVVTDAFFNGIKNQA
GSGCEGKNFYTRSAFLSAVNAYPG
FAHGGTEVEGKREIAAFFAHVTHE
TGHFCYISEINKSNAYCDASNRQW
PCAAGQKYYGRGPLQISWNYNYGP
AGRDIGFNGLADPNRVAQDAVIAF
KTALWFWMNNVHRVMPQGFGATIR
AINGALECNGNNPAQMNARVGYYK
QYCQQLRVDPGPNLIC
chitinase (EC Zea mays 268 QLVALGLALLCAVAGPAAAQNCGC
3.2.1.14) QPNVCCSKFGYCGTTDEYCGDGCQ
precursor SGPCRSGRGGGGSGGGGANVASVV
TSSFFNGIKNQAGSGCEGKNFYTR
SAFLSAVKGYPGFAHGGSQVQGKR
EIAAFFAHATHETGHFCYISEINK
SNAYCDPTKRQWPCAAGQKYYGRG
PLQISWNYNYGPAGRAIGFDGLGD
PGRVARDAVVAFKAALWFWMNSVH
GVVPQGFGATTRAMQRALECGGNN
PAQMNARVGYYRQYCRQLGVDPGP
NLTC
Chitinase, Nicotiana 377 MANSVTLFAIIFSCFLLQQLVCTN
class V tabacum SQNVKGGYWFKDSGLALNNIDSTL
ETHLFCAFADLNPQLNQLIISPEN
QDSFRQFTSTVQRKNPSVKTFLSI
AGGRANSTAYGIMARQPNSRKSFI
DSSIRLARQLGFHGLDLDWEYPLS
AADMTNLGTLLNEWRTAINTEARN
SGRAALLLTAAVSNSPRVNGLNYP
VESLARNLDWINLMAYDFYGPNWS
PSQTNSHAQLFDPVNHVSGSDGIN
AWIQAGVPTKKLVLGIPFYGYAWR
LVNANIHGLRAPAAGKSNVGAVDD
GSMTYNRIRDYIVESRATTVYNAT
IVGDYCYSGSNWISYDDTQTVRNK
VNYVKGRGLLGYFAWHVAGDQNWG
LSRTASQTWGVSFQEMK
Chitin- Hydrangea 15 NSMERVEELRKKLQD
binding macrophylla
protein HM30
(Fragment)
Chitin-binding Hordeum 52 ATYHYYRPAQNNWDLGAPAVSAYC
protein N, CBP vulgare ATWDASKYGWTAFIVDQCANGGLD
N (Fragments) LDWN
Circulin A Chassalia 30 GIPCGESCVWIPCISAALGCSCKN
(CIRA) parviflora KVCYRN
Circulin B Chassalia 31 GVIPCGESCVFIPCISTLLGCSCK
(CIRB) parviflora NKVCYRN
Cyclo- Psychotria 31 SIPCGESCVFIPCTVTALLGCSCK
psychotride A longipes SKVCYKN
(CPT)
Cysteine-rich Brassica 27 QKLCERPSGTWSGVCGNNNACKNQ
antifungal rapa CIN
protein 1
(AFP1)
(Fragment)
Cysteine-rich Sinapis alba 51 QKLCERPSGTWSGVCGNNNACKNQ
antifungal CINLEKARHGSCNYVFPAHKCICY
protein 1 FPC
(AFP1) (M1)
Cysteine-rich Raphanus 80 MAKFASIIALLFAALVLFAAFEAP
antifungal sativus TMVEAQKLCERPSGTWSGVCGNNN
protein 1 ACKNQCINLEKARHGSCNYVFPAH
precursor KCICYFPC
(AFP1)
Cysteine-rich Arabidopsis 80 MAKSATIVTLFFAALVFFAALEAP
antifungal thaliana MVVEAQKLCERPSGTWSGVCGNSN
protein 1 ACKNQCINLEKARHGSCNYVFPAH
precursor KCICYFPC
(AFP1)
(Anther-
specific
protein S18
homolog)
Cysteine-rich Brassica 23 QKLCERPSGTWSGVCGNNNACKN
antifungal napus
protein 2
(AFP2)
(Fragment)
Cysteine-rich Brassica 27 QKLCERPSGTXSGVCGNNNACKNQ
antifungal rapa CIR
protein 2
(AFP2)
(Fragment)
Cysteine-rich Raphanus 80 MAKFASIIVLLFVALVVFAAFEEP
antifungal sativus TMVEAQKLCQRPSGTWSGVCGNNN
protein 2 ACKNQCIRLEKARHGSCNYVFPAH
precursor KCICYFPC
(AFP2)
Cysteine-rich Sinapis alba 51 QKLCQRPSGTWSGVCGNNNACRNQ
antifungal CINLEKARHGSCNYVFPAHKCICY
protein 2A FPC
(AFP2A) (M2A)
Cysteine-rich Sinapis alba 52 QKLCARPSGTWNSSGNCRNNNACR
antifungal NFCIKLEKSRHGSCNIPFPSNKCI
protein 2B CYFPC
(AFP2B) (M2B)
Cysteine-rich Brassica 79 MAKFASIITLLFAALVVFAAFEAP
antifungal napus TMVEAKLCERSSGTWSGVCGNNNA
protein 3 CKNQCIRLEGAQHGSCNYVFPAHK
precursor CICYFPC
(AFP3)
Cysteine-rich Raphanus 79 MAKFASIVALLFAALVVFAAFEAP
antifungal sativus TVVEAKLCERSSGTWSGVCGNNNA
protein 3 CKNQCIRLEGAQHGSCNYVFPAHK
precursor CICYFPC
(AFP3)
Cysteine-rich Raphanus 80 MAKFVSIITLLFVALVLFAAFEAP
antifungal sativus TMVEAQKLCERSSGTWSGVCGNNN
protein 4 ACKNQCINLEGARHGSCNYIFPYH
precursor RCICYFPC
(AFP4)
Defense- Pisum 46 KTCEHLADTYRGVCFTNASCDDHC
related sativum KNKAHLISGTCHNWKCFCTQNC
peptide 1
(Defensin 1)
(Antifungal
protein Psd1)
Defense- Pisum 47 KTCENLSGTFKGPCIPDGNCNKHC
related sativum RNNEHLLSGRCRDDFRCWCTNRC
peptide 2
(Defensin 2)
(Antifungal
protein Psd2)
defensin Capsicum 75 MAGFSKVIATIFLMMMLVFATDMM
annuum AEAKICEALSGNFKGLCLSSRDCG
NVCRREGFTSGVCRGFPLKCFCRK
PGA
Defensin Brassica 80 MAKFVSIITLFFAALVLFAAFEAP
rapa TMVKAQKLCERSSGTWSGVCGNNN
ACKNQCINLEGARHGSCNYVFPYH
RCICYFPC
Defensin Helianthus 108 MAKISVAFNAFLLLLFVLAISEIG
annuus SVKGELCEKASQTWSGTCGKTKHC
DDQCKSWEGAAHGACHVRDGKHMC
FCYFNCSKAQKLAQDKLRAEELAK
EKIEPEKATAKP
Defensin Helianthus 41 SHRFQGTCLSDTNCANVCHSERFS
(Fragment) annuus GGKCRGFRRRCFCTTHC
defensin 1 Triticum 82 MASTRRMAAAPAVLLLLLLLVATE
precursor aestivum MGTMKTAEARTCLSQSHKFKGTCL
SNSNCAAVCRTENFPDGECNTHLV
ERKCYCKRTC
defensin AFP1 Heuchera 54 DGVKLCDVPSGTWSGHCGSSSKCS
sanguinea QQCKDREHFAYGGACHYQFPSVKC
FCKRQC
defensin AMP1 Dahlia 50 ELCEKASKTWSGNCGNTGHCDNQC
merckii KSWEGAAHGACHVRNGKHMCFCYF
NC
defensin AMP1 Aesculus 50 LCNERPSQTWSGNCGNTAHCDKQC
hippocastanum QDWEKASHGACHKRENHWKCFCYF
NC
defensin AMP1 Clitoria 49 NLCERASLTWTGNCGNTGHCDTQC
ternatea RNWESAKHGACHKRGNWKCFCYFN
C
defensin AMP2 Dahlia 20 EVCEKASKTWSGNCGNTGHC
merckii
Defensin CUA1 Helianthus 42 LSHSFKGTCLSDTNCANVCHSERF
(Fragment) annuus SGGKCRGFRRRCFCTTHC
Defensin Elaeis 77 MEHSRRMLPAILLLLFLLMPSEMG
EGAD1 guineensis TKVAEARTCESQSHKFQGTCLRES
NCANVCQTEGFQGGVCRGVRRRCF
CTRLC
Defensin J1-1 Capsicum 75 MAGFSKVVATIFLMMLLVFATDMM
precursor annuum AEAKICEASGNFKGLCLSSRDCGN
VCRREGFTDGSCIGFRLQCFCTKP
CA
Defensin J1-2 Capsicum 74 MAGFSKVIATIFLMMMLVFATGMV
precursor annuum AEARTCESQSHRFKGLCFSKSNCG
SVCHTEGFNGGHCRGFRRRCFCTR
HC
Defensin Brassica 80 MAKVASIVALLFPALVIFAAFEAP
precursor oleracea TMVEAQKLCERPSGWNSGVCGNN
NACKNQCIRLEKARHGSCNYVFPA
HKCICYFPC
Defensin Prunus 79 MERSMRLFSTAFVFFLLLAAAGMM
protein 1 persica MGPMVAEARTCESQSNRFKGTCVS
TSNCASVCQTEGFPGGHCRGFRRR
CFCTKHC
Endochitinase Zea mays 280 MANAPRILALGLLALLCAAAGPAA
A precursor AQNCGCQPNFCCSKFGYCGTTDAY
(EC 3.2.1.14) CGDGCQSGPCRSGGGGGGGGGGGG
(Seed GGSGGANVANVVTDAFFNGIKNQA
chitinase A) GSGCEGKNFYTRSAFLSAVNAYPG
FAHGGTEVEGKREIAAFFAHVTHE
TGHFCYISEINKSNAYCDASNRQW
PCAAGQKYYGRGPLQISWNYNYGP
AGRDIGFNGLADPNRVAQDAVIAF
KTALWFWMNNVHGVMPQGFGATIR
AINGALECNGNNPAQMNARVGYYK
QYCQQLRVDPGPNLIC
Endochitinase Zea mays 269 PQLVALGLALLCAVAGPAAAQNCG
B precursor CQPNVCCSKFGYCGTTDEYCGDGC
(EC 3.2.1.14) QSGPCRSGRGGGGSGGGGANVASV
(Seed VTSSFFNGIKNQAGSGCEGKNFYT
chitinase B) RSAFLSAVKGYPGFAHGGSQVQGK
(Fragment) REIAAFFAHATHETGHFCYISEIN
KSNAYCDPTKRQWPCAAGQKYYGR
GPLQISWNYNYGPAGRAIGFDGLG
DPGRVARDAVVAFKAALWFWMNSV
HGVVPQGFGATTRAMQRALECGGN
NPAQMNARVGYYRQYCRQLGVDPG
PNLTC
Fabatin-1 Vicia faba 47 LLGRCKVKSNRFHGPCLTDTHCST
VCRGEGYKGGDCHGLRRRCMCLC
Fabatin-2 Vicia faba 47 LLGRCKVKSNRFNGPCLTDTHCST
VCRGEGYKGGDCHGLRRRCMCLC
Floral Petunia x 103 MARSICFFAVAILALMLFAAYDAE
defensin-like hybrida AATCKAECPTWDSVCINKKPCVAC
protein 1 CKKAKFSDGHCSKILRRCLCTKEC
VFEKTEATQTETFTKDVNTLAEAL
LEADMMV
Floral Petunia x 101 MARSICFFAVAILALMLFAAYETE
defensin-like hybrida AGTCKAECPTWEGICINKAPCVKC
protein 2 CKAQPEKFTDGHCSKILRRCLCTK
PCATEEATATLANEVKTMAEALVE
EDMME
Flower- Helianthus 78 MKSSMKMFAALLLVVMCLLANEMG
specific annuus GPLVVEARTCESQSHKFKGTCLSD
gamma-thionin TNCANVCHSERFSGGKCRGFRRRC
precursor FCTTHC
(Defensin
SD2)
Gamma-thionin Arabidopsis 77 MKLSMRLISAVLIMFMIFVATGMG
homolog thaliana PVTVEARTCESQSHRFKGTCVSAS
At2g02100 NCANVCHNEGFVGGNCRGFRRRCF
precursor CTRHC
Gamma-thionin Arabidopsis 77 MKFSMRLISAVLFLVMIFVATGMG
homolog thaliana PVTVEARTCASQSQRFKGKCVSDT
At2g02120 NCENVCHNEGFPGGDCRGFRRRCF
precursor CTRNC
Gamma-thionin Arabidopsis 77 MKLSVRFISAALLLFMVFIATGMG
homolog thaliana PVTVEARTCESKSHRFKGPCVSTH
At2g02130 NCANVCHNEGFGGGKCRGFRRRCY
precursor CTRHC
Gamma-thionin Arabidopsis 73 MKLSLRLISALLMSVMLLFATGMG
homolog thaliana PVEARTCESPSNKFQGVCLNSQSC
At2g02140 AKACPSEGFSGGRCSSLRCYCSKA
precursor C
Gamma- Eutrema 80 MAKFASIIALLFAALVLFSAFEAP
thionin 1 wasabi SMVEAQKLCEKSSGTWSGVCGNNN
precursor ACKNQCINLEGARHGSCNYIFPYH
RCICYFPC
gamma- Lycopersicon 105 MARSIFFMAFLVLAMMLFVTYEVE
thionin-like esculentum AQQICKAPSQTFPGLCFMDSSCRK
protein YCIKEKFTGGHCSKLQRKCLCTKP
precursor CVFDKISSEVKATLGEEAKTLSEW
LEEEIMME
Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI
MGM protein elata PAFASDRLNSGHQLDTGGSLAQGG
YLFIIQNDCNLVLYDNNRAVWASG
TNGKASGCMLKMQNDGNLVIYSGS
RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT
VIPHSNGTAAASGAAQNKVNELYI
SMY
Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI
MNF protein elata PAFASDRLNSGHQLDTGGSLAQGG
YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS
RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT
VIPHSNGTAAASGAAQNKVNELYI
SMY
Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTVMSLSAI
VGM protein elata PAFASDRLNSGHQLDTGGSLAQGG
YLFIIQNDCNLVLYDNNRAVWASG
TNGKASGCMLKMQNDGNLVIYSGS
RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT
VIPHSNGTAAASGAAQNKVNELYI
SMY
Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTVMSLSAI
VNF protein elata PAFASDRLNSGHQLDTGGSLAQGG
YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS
RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT
VIPHSNGTAAASGAAQNKVNELYI
SMY
Genomic DNA, Arabidopsis 73 MENKFFAAFFLLLVLFSSQEIIGG
chromosome 5, thaliana EGRTCQSKSHHFKYMCTSNHNCAI
P1 clone:MBK5 VCRNEGFSGGRCHGFHRRCYCTRL
C
Ginkbilobin Ginkgo 40 ANTAFVSSAHNTQKIPAGAPFNRN
(GNL) biloba LRAMLADLRQNAAFAG
(Fragment)
Hevein Hevea 204 MNIFIVVLLCLTGVAIAEQCGRQA
precursor brasiliensis GGKLCPNNLCCSQWGWCGSTDEYC
(Major SPDHNCQSNCKDSGEGVGGGSASN
hevein) VLATYHLYNSQDHGWDLNAASAYC
[Contains: STWDANKPYSWRSKYGWTAFCGPV
Hevein GAHGQSSCGKCLSVTNTGTGAKTT
(Allergen Hev VRIVDQCSNGGLDLDVNVFRQLDT
b 6); Win- DGKGYERGHITVNYQFVDCGDSFN
like protein] PLFSVMKSSVIN
hevein-like Euonymus 320 MKYLWVFIVFSIAVLSHACSAQQC
antimicrobial europaeus GRQAGNRRCANNLCCSQYGYCGRT
peptide NEYCCTSQGCQSQCRRCGVRTVGE
IVVGDIGGIISKGMFNNILKHRDD
DACEGKGFYTYEAFVAAARSFPAF
GSTGDDATRKREIAAFLAQTSHET
SAGWPSAPDGPYAWGYCFVRERNP
PSKYCDTTTPCPKSYYGRGPIQLT
WNYNYEQAGRAIGADLLNNPDLVA
TDAVISFKTAIWFWMTAQSSKPSC
HDVITGSWRPSASDNSVCHVPDYA
VVTNIISGEIEYGKSRNPQVEDRI
EFFKRYCQILGVSPGKCYEERTFV
SGLMMETI
hevein-like Euonymus 305 MKYLWVFIVFSIAVLSLACSAQQC
antimicrobial europaeus GRQAGNRRCPNNLCCSQFGYCGRT
peptide NEYCCTGFGCQSNCRRCGVRTVGE
DVVGDIGGIISKGMFNNILKHRDD
DACEGKGFYTYEAFVAAARSFPAF
GSTGDDTTRKREIAAFLAQTSHET
SGGRPSAPDGPYAWGYCFVKERNP
PSKYCDTITPCPKSYYGRGPLQLT
WNYNYAQAGRAIGVDLLNNPDLVA
TDAVTSFKTAIWFWMTAHSSKPSC
HDVITGSWRPSASDNSVRHVPDYA
VVTNIINGEIEYGKSRNPQVEDRI
EFFKRYCQILGVSPGKF
Leaf-specific Hordeum 137 MAPSKSIKSVVICVLILGLVLEQV
thionin vulgare QVEGKSCCKDTLARNCYNTCHFAG
precursor GSRPVCAGACRCKIISGPKCPSDY
(Clone DB4) PKLNLLPESGEPDVTQYCTIGCRN
SVCDNMDNVFRGQEMKFDMGLCSN
ACARFCNDGAVIQSVEA
Lectin-like Gastrodia 111 QSSPGILLNQPASMASPASSAVIF
protein elata FFAVAALMSLLAMPALAASQLNAG
(Fragment) QTLGTGQSLAQGPNQFIIQNDCNL
VLYASNKAVWATGTNGKASGCVLR
MQRDGNLVIYSGSKV
Nicotiana Nicotiana 47 RECKTESNTFPGICITKPPCRKAC
Alata Plant tabacum ISEKFTDGHCSKILRRCLCTKPC
Defensin 1
(Nad1)
osmotin Nicotiana 250 MSNNMGNLRSSFVFFLLALVTYTY
precursor tabacum AATIEVRNNCPYTVWAASTPIGGG
RRLDRGQTWVINAPRGTKMARVWG
RTNCNFNAAGRGTCQTGDCGGVLQ
CTGWGKPPNTLAEYALDQFSGLDF
WDISLVDGFNIPMTFAPTNPSGGK
CHAIHCTANINGECPRELRVPGGC
NNPCTTFGGQQYCCTQGPCGPTFF
SKFFKQRCPDAYSYPQDDPTSTFT
CPGGSTNYRVIFCPNGQAHPNFPL
EMPGSDEVAK
Osmotin-like Nicotiana 251 MSHLTTFLVFFLLAFVTYTYASGV
protein tabacum FEVHNNCPYTVWAAATPVGGGRRL
precursor ERGQSWWFWAPPGTKMARIWGRTN
(Patho- CNFDGAGRGWCQTGDCGGVLECKG
genesis- WGKPPNTLAEYALNQFSNLDFWDI
related SVIDGFNIPMSFGPTKPGPGKCHG
protein PR- IQCTANINGECPGSLRVPGGCNNP
5D) CTTFGGQQYCCTQGPCGPTELSRW
FKQRCPDAYSYPQDDPTSTFTCTS
WTTDYKVMFCPYGSAHNETTNFPL
EMPTSTHEVAK
Osmotin-like Lycopersicon 238 FFFLLAFVTYTYAATFEVRNNCPY
protein TPM-1 esculentum TVWAASTPIGGGRRLDRGQTWVIN
precursor (PR APRGTKMARIWGRTNCNFDGDGRG
P23) SCQTGDCGGVLQCTGWGKPPNTLA
(Fragment) EYALDQFSNLDFWDISLVDGFNIP
MTFAPTNPSGGKCHAIHCTANING
ECPGSLRVPGGCNNPCTTFGGQQY
CCTQGPCGPTDLSRFFKQRCPDAY
SYPQDDPTSTFTCPSGSTNYRVVF
CPNGVTSPNFPLEMPSSDEEAK
pathogenesis- Lycopersicon 233 AFVTYTYAATFEVRNNCPYTVWAA
related esculentum STPIGGGRRLDRGQTWVINAPRGT
protein P23 KMARIWGRTNCNFDGAGRGSCQTG
precursor DCGGVLQCTGWGKPPNTLAEYALD
QFSNLDFWDISLVDGFNIPMTFAP
TNPSGGKCHAIHCTANINGECPGS
LRVPGGCNNPCTTFGGQQYCCTQG
PCGPTDLSRFFKQRCPDAYSYPQD
DPTSTFTCPSGSTNYRVVFCPNGV
TSPNFPLEMPSSDEEAK
plant Arabidopsis 76 MKVSPRLNSALLLLFMILATVMGL
defensin thaliana VTVEARTCETSSNLFNGPCLSSSN
protein, CANVCHNEGFSDGDCRGFRRRCLC
putative TRPC
(PDF2.4)
plant Arabidopsis 122 MERIPSLASLVSLLIIFATVVNQT
defensin- thaliana RASICNDRLGLCDGCDQRCKAKHG
fusion PSCESKCDGPVGMLLCTCTYECGP
protein, TKLCNGGLGNCGESCNEQCCDRNC
putative AQRYNGGHGYCNTLDDFSLCLCKY
PC
Plant Pyrus 81 LVSTAFVLVLLLATIEMGPMGVEA
defensin-like pyrifolia RTESSKAVEGKICEVPSTLFKGLC
protein FSSNNCKHTCRKEQFTRGHCSVLT
(Fragment) RACVCTKKC
probable Arabidopsis 80 MAKFCTTITLILVALVLFADFEAP
antifungal thaliana TIVKAELCKRESETWSGRCVNDYQ
protein CRDHCINNDRGNDGYCAGGYPWYR
[imported] SCFCFFSC
Probable Arabidopsis 80 MAKSAAIITFLFAALVLFAAFEAP
cysteine-rich thaliana IMVEAQKLCEKPSGTWSGVCGNSN
antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein KCICYFPC
At2g26010
precursor
(AFP)
Probable Arabidopsis 80 MAKFASIITFIYAALVLFAAFEVP
cysteine-rich thaliana TMVEAQKLCEKPSGTWSGVCGNSN
antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein KCICYVPC
At2g26020
precursor
(AFP)
Probable Arabidopsis 80 MAKFASIITLIFAALVLFAAFDAP
cysteine-rich thaliana AMVEAQKLCEKPSGTWSGVCGNSN
antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein LCR77 KCICYVPC
precursor
(AFP)
Protease Pyrus 87 MEPSMRLISAAFVLILLLATTEMG
inhibitor- pyrifolia PMGVEAKSKSSKEVEKRTCEAASG
like protein KFKGMCFSSNNCANTCAREKFDGG
KCKGFRRRCMCTKKC
Protease Pyrus 87 MERSMRLVSAAFVLVLLLAATEMG
inhibitor- pyrifolia PMGVEARTESSKAVEGKICEVPST
like protein LFKGLCFSSNNCKHTCRKEQFTRG
HCSVLTRACVCTKKC
Proteinase Capsicum 78 MAHSMRFFAIVLLLAMLVMATEMG
inhibitor annuum PMRIVEARTCESQSHRFKGVCASE
precursor TNCASVCQTEGFSGGDCRGFRRRC
FCTRPC
Putative Arabidopsis 78 MASSYTLMLFLCLSIFLIASTEMM
defensin AMP1 thaliana AVEGRICERRSKTWTGFCGNTRGC
protein DSQCKRWERASHGACHAQFPGFAC
FCYFNC
Putative Picea abies 83 MADKGVGSRLSALFLLVLLVISIG
plant MMQLEPAEGRTCKTPSGKFKGVCA
defensin SRNNCKNVCQTEGFPSGSCDFHVA
SPI1B NRKCYCSKPCP
sormatin Sorghum 22 AVFTVVNRCPYTVWAASVPVGG
bicolor
TOM P14A Lycopersicon 41 AVHNDARAQVGVGPMSXDANLASR
protein esculentum AQNYANSRAXDXNLIXS
(Fragment)
TOM P14B Lycopersicon 35 DXLAVHNDARAQVGAGPMDANLAS
pathogenesis- esculentum RAQNXANSRAG
related PR-1
protein
(Fragments)
TOM P14C Lycopersicon 97 DYLNAHNAARRQVGVGPMTXDNRL
pathogenesis- esculentum AAFAQNYANQRADXRMQHSGGPYG
related PR-1 ENLAAAFPQLNCQAGKVCGHYTQV
protein VWRNSVRLGCARVRCNNGWYFITC
(Fragments) N
trimatin Triticum 23 ATITVVNRCSYTVWPGALPGGGA
aestivum
Vicilin Macadamia 666 MAINTSNLCSLLFLLSLFLLSTTV
integrifolia SLAESEFDRQEYEECKRQCMQLET
SGQMRRCVSQCDKRFEEDIDWSKY
DNQDDPQTDCQQCQRRCRQQESGP
RQQQYCQRRCKEICEEEEEYNRQR
DPQQQYEQCQERCQRHETEPRHMQ
TCQQRCERRYEKEKRKQQKRYEEQ
QREDEEKYEERMKEEDNKRDPQQR
EYEDCRRRCEQQEPRQQYQCQRRC
REQQRQHGRGGDLINPQRGGSGRY
EEGEEKQSDNPYYFDERSLSTRFR
TEEGHISVLENFYGRSKLLRALKN
YRLVLLEANPNAFVLPTHLDADAI
LLVTGGRGALKMIHRDNRESYNLE
CGDVIRIPAGTTFYLINRDNNERL
HIAKFLQTISTPGQYKEFFPAGGQ
NPEPYLSTFSKEILEAALNTQAER
LRGVLGQQREGVIISASQEQIREL
TRDDSESRRWHIRRGGESSRGPYN
LFNKRPLYSNKYGQAYEVKPEDYR
QLQDMDVSVFIANITQGSMMGPFF
NTRSTKVVVVASGEADVEMACPHL
SGRHGGRRGGKRHEEEEDVHYEQV
KARLSKREAIVVPVGHPVVFVSSG
NENLLLFAFGINAQNNHENFLAGR
ERNVLQQIEPQAMELAFAAPRKEV
EELFNSQDESIFFPGPRQHQQQSS
RSTKQQQPLVSILDFVGF
Vicilin Macadamia 666 MAINTSNLCSLLFLLSLFLLSTTV
integrifolia SLAESEFDRQEYEECKRQCMQLET
SGQMRRCVSQCDKRFEEDIDWSKY
DNQEDPQTECQQCQRRCRQQESGP
RQQQYCQRRCKEICEEEEEYNRQR
DPQQQYEQCQKHCQRRETEPRHMQ
TCQQRCERRYEKEKRKQQKRYEEQ
QREDEEKYEERMKEEDNKRDPQQR
EYEDCRRRCEQQEPRQQHQCQLRC
REQQRQHGRGGDMMNPQRGGSGRY
EEGEEEQSDNPYYFDERSLSTRFR
TEEGHISVLENFYGRSKLLRALKN
YRLVLLEANPNAFVLPTHLDADAI
LLVIGGRGALKMIHHDNRESYNLE
CGDVIRIPAGTTFYLINRDNNERL
HIAKFLQTISTPGQYKEFFPAGGQ
NPEPYLSTFSKEILEAALNTQTEK
LRGVFGQQREGVIIRASQEQIREL
TRDDSESRHWHIRRGGESSRGPYN
LFNKRPLYSNKYGQAYEVKPEDYR
QLQDMDLSVFIANVTQGSMMGPFF
NTRSTKVVVVASGEADVEMACPHL
SGRHGGRGGGKRHEEEEDVHYEQV
RARLSKREAIVVLAGHPVVFVSSG
NENLLLFAFGINAQNNHENFLAGR
ERNVLQQIEPQAMELAFAAPRKEV
EESFNSQDQSIFFPGPRQHQQQSP
RSTKQQQPLVSILDFVGF
Vicilin Macadamia 625 QCMQLETSGQMRRCVSQCDKRFEE
(Fragment) integrifolia DIDWSKYDNQEDPQTECQQCQRRC
RQQESDPRQQQYCQRRCKEICEEE
EEYNRQRDPQQQYEQCQKRCQRRE
TEPRHMQICQQRCERRYEKEKRKQ
QKRYEEQQREDEEKYEERMKEGDN
KRDPQQREYEDCRRHCEQQEPRLQ
YQCQRRCQEQQRQHGRGGDLMNPQ
RGGSGRYEEGEEKQSDNPYYFDER
SLSTRFRTEEGHISVLENFYGRSK
LLRALKNYRLVLLEANPNAFVLPT
HLDADAILLVIGGRGALKMIHRDN
RESYNLECGDVIRIPAGTTFYLIN
RDNNERLHIAKFLQTISTPGQYKE
FFPAGGQNPEPYLSTFSKEILEAA
LNTQTERLRGVLGQQREGVIIRAS
QEQIRELTRDDSESRRWHIRRGGE
SSRGPYNLFNKRPLYSNKYGQAYE
VKPEDYRQLQDMDVSVFIANITQG
SMMGPFFNTRSTKVVVVASGEADV
EMACPHLSGRHGGRGGGKRHEEEE
EVHYEQVRARLSKREAIVVLAGHP
VVFVSSGNENLLLFAFGINAQNNH
ENFLAGRERNVLQQIEPQAMELAF
AASRKEVEELFNSQDESIFFPGPR
QHQQQSPRSTKQQQPLVSILDFVG
F
Wheatwin1 Triticum 146 MAARPMLVVALLCAAAAAATAQQA
precursor aestivum TNVRATYHYYRPAQNNWDLGAPAV
(Patho- SAYCATWDASKPLSWRSKYGWTAF
genesis- CGPAGAHGQASCGKCLQVTNPATG
related AQITARIVDQCANGGLDLDWDTVF
protein 4a) TKIDTNGIGYQQGHLNVNYQFVDC
(Protein RD
0.14)
Wheatwin2 Triticum 148 MTMAARLMLVAALLCAAAAAATAQ
precursor aestivum QATNVRATYHYYRPAQNNWDLGAP
(Patho- AVSAYCATWDASKPLSWRSKYGWT
genesis- AFCGPAGAHGQAACGKCLRVTNPA
related TGAQITARIVDQCANGGLDLDWDT
protein 4b) VFTKIDTNGIGYQQGHLNVNYQFV
DCRD
Zeamatin Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGR
QLNRGESWRITAPAGTTAARIWAR
TGCKFDASGRGSCRTGDCGGVLQC
TGYGRAPNTLAEYALKQFNNLDFF
DISLIDGFNVPMSFLPDGGSGCSR
GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANDCHPTN
YSRYFKGQCPDAYSYPKDDATSTF
TCPAGTNYKVVFCP
Zeamatin Zea mays 227 MAGSVAIVGIFVALLAVAGEAAVF
precursor TVVNQCPFTVWAASVPVGGGRQLN
RGESWRITAPAGTTAARIWARTGC
KFDASGRGSCRTGDCGGVLQCTGY
GRAPNTLAEYALKQFNNLDFFDIS
LIDGFNVPMSFLPDGGSGCSRGPR
CAVDVNARCPAELRQDGVCNNACP
VFKKDEYCCVGSAANDCHPTNYSR
YFKGQCPDAYSYPKDDATSTFTCP
AGTNYKVVFCP
TABLE 2
{PRIVATE} Defensins
Name Organism Sequence
HNP-1 Human ACYCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-2 Human CYCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-3 Human DCYCRIPACIAGERRYGTCIYQGRLWAFCC
HNP-4 Human VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV
NP-1 Rabbit VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR
NP-2 Rabbit VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR
NP-3A Rabbit GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR
NP-3B Rabbit GRCVCRKQLLCSYRERRIGDCKIRGVRFPFCCPR
NP-4 Rabbit VSCTCRRFSCGFGERASGSCTVNGVRHTLCCRR
NP-5 Rabbit VFCTCRGFLCGSGERASGSCTINGVRHTLCCRR
RatNP-1 Rat VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR
Rat-NP-3 Rat CSCRYSSCRFGERLLSGACRLNGRIYRLCC
Rat-NP-4 Rat ACTCRIGACVSGERLTGACGLNGRIYRLCCR
GPNP Guinea pig RRCICTTRTCRFPYRRLGTCIFQNRVYTFCC
B. Growth Factors
In some embodiments of the present invention, trophic factor combinations for treating injured nervous systems comprise one or more growth factors. Growth factors useful in the present invention include, but are not limited to, the following broad classes of cytoactive compounds: Insulin, Insulin like growth factors such as IGF-I, IGF-IB, IGF-II, and IGF-BP; Heparin-binding growth factors such as Pleiotrophin (NEGF1) and Midkine (NEGF2); PC-cell derived growth factors (PCDGF); Epidermal Growth Factors such as α-EGF and β-EGF; EGF-like molecules such as Keratinocyte-derived growth factor (which is identical to KAF, KDGF, and amphiregulin) and vaccinia virus growth factor (VVGF); Fibroblast Growth Factors such as FGF-1 (Basic FGF Protein), FGF-2 (Acidic FGF Protein), FGF-3 (Int-2), FGF-4 (Hst-1), FGF-5, FGF-6, and FGF-7 (identical to KGF); FGF-Related Growth Factors such as Endothelial Cell Growth Factors (e.g., ECGF-α and ECGF-β); FGF- and ECGF-Related Growth Factors such as Endothelial cell stimulating angiogenesis factor and Tumor angiogenesis factor, Retina-Derived Growth Factor (RDGF), Vascular endothelium growth factors (VEGF, VEGF-B, VEGF-C, and VEGF-D), Brain-Derived Growth Factor (BDGF A- and -B), Astroglial Growth Factors (AGF 1 and 2), Omentum-derived factor (ODF), Fibroblast-Stimulating factor (FSF), and Embryonal Carcinoma-Derived Growth Factor; Neurotrophic Growth Factors such as α-NGF, β-NGF, γ-NGF, Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF); Glial Growth Factors such as GGF-I, GGF-II, GGF-III, Glia Maturation Factor (GMF), and Glial-Derived Nuerotrophic Factor (GDNF); Organ-Specific Growth Factors such as Liver Growth Factors (e.g., Hepatopoietin A, Hepatopoietin B, and Hepatocyte Growth Factors (HCGF or HGF), Prostate Growth Factors (e.g., Prostate-Derived Growth Factors [PGF] and Bone Marrow-Derived Prostate Growth Factor), Mammary Growth Factors (e.g., Mammary-Derived Growth Factor 1 [MDGF-1] and Mammary Tumor-Derived Factor [MTGF]), and Heart Growth Factors (e.g., Nonmyocyte-Derived Growth Factor [NMDGF]); Cell-Specific Growth Factors such as Melanocyte Growth Factors (e.g., Melanocyte-Stimulating Hormone [α-, β-, and γ-MSH] and Melanoma Growth-Stimulating Activity [MGSA]), Angiogenic Factors (e.g., Angiogenin, Angiotropin, Platelet-Derived ECGF, VEGF, and Pleiotrophin), Transforming Growth Factors (e.g., TGF-α, TGF-β, and TGF-like Growth Factors such as TGF-β2, TGF-β3, TGF-e, GDF-1, GDF-9, CDGF and Tumor-Derived TGF-β-like Factors), ND-TGF, and Human epithelial transforming factor [h-TGFe]); Regulatory Peptides with Growth Factor-like Properties such as Bombesin and Bombesin-like peptides (e.g., Ranatensin, and Litorin], Angiotensin, Endothelin, Atrial Natriuretic Factor, Vasoactive Intestinal Peptide, and Bradykinin; Cytokines such as connective tissue growth factor (CTGF), the interleukins IL-1 (e.g., Osteoclast-activating factor (OAF), Lymphocyte-activating factor (LAF), Hepatocyte-stimulating factor (HSF), Fibroblast-activating factor (FAF), B-cell-activating factor (BAF), Tumor inhibitory factor 2 (TIF-2), Keratinocyte-derived T-cell growth factor (KD-TCGF)), IL-2 (T-cell growth factor (TCGF), T-cell mitogenic factor (TCMF)), IL-3 (e.g., Hematopoietin, Multipotential colony-stimulating factor (multi-CSF), Multilineage colony-stimulating activity (multi-CSA), Mast cell growth factor (MCGF), Erythroid burst-promoting activity (BPA-E), IL-4 (e.g., B-cell growth factor I (BCGF-I), B-cell stimulatory factor I (BSF-1)), IL-5 (e.g., B-cell growth factor II (BCGF-II), Eosinophil colony-stimulating factor (Eo-CSF), Immunoglobulin A-enhancing factor (IgA-EF), T-cell replacing factor (TCRF)), IL-6 (B-cell stimulatory factor 2 (BSF-2), B-cell hybridoma growth factor (BCHGF), Interferon β2 (IFN-B), T-cell activating factor (TAF), IL-7 (e.g., Lymphopoietin 1 (LP-1), Pre-B-cell growth factor (pre-BCGF)), IL-8 (Monocyte-derived neutrophil chemotacetic factor (MDNCF), Granulocyte chemotatic factor (GCF), Neutrophil-activating peptide 1 (NAP-1), Leukocyte adhesion inhibitor (LAI), T-lymphocyte chemotacetic factor (TLCF)), IL-9 (e.g., T-cell growth factor III (TCGF-III), Factor P40, MegaKaryoblast growth factor (MKBGF), Mast cell growth enhancing activity (MEA or MCGEA)), IL-10 (e.g., Cytokine synthesis inhibitory factor (CSIF)), IL-11 (e.g., Stromal cell-derived cytokine (SCDC)), IL-12 (e.g., Natural killer cell stimulating factor (NKCSF or NKSF), Cytotoxic lymphocyte maturation factor (CLMF)), TNF-α (Cachectin), TNF-β (Lymphotoxin), LIF (Differentiation-inducing factor (DIF), Differentiation-inducing activity (DIA), D factor, Human interleukin for DA cells (HILDA), Hepatocyte stimulating factor III (HSF-III), Cholinergic neuronal differentiation factor (CNDF), CSF-1 (Macrophage colony-stimulating factor (M-CSF)), CSF-2 (Granulocyte-macrophage colony-stimulating factor (GM-CSF)), CSF-3 (Granulocyte colony-stimulating factor (G-CSF)), and erythropoietin; Platelet-derived growth factors (e.g., Placental growth factor (PlGF), PDGF-A, PDGF-B, PDGF-AB, p28-sis, and p26-cis), and Bone Morphogenetic proteins (e.g., BMP and BMP-15), neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y), and neurotransmitters (e.g., norepinephrine and acetylcholine).
Suitable growth factors may be obtained from commercial sources, purified from natural sources, or be produced by recombinant methods. Recombinant growth factors can be produced from wild-type coding sequences or from variant sequences that encode functional growth factors. Suitable growth factors also include analogs that may be smaller peptides or other molecules having similar binding and biological activity as the natural growth factors. Methods for producing growth factors are described in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.
C. Neurotrophins
The trophic factor combinations provided herein also can include one or more neurotrophic growth factors such as Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF).
Nerve growth factor s, such as α-NGF, β-NGF, γ-NGF, and the like, are neurotrophins. In an embodiment, the trophic factor combination does not include a nerve growth factor, which results in lessened pain.
D. Neuropeptides
The trophic factor combinations provided herein also can include one or more neuropeptides, e.g., PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide (MAB-alpha-NP); Beta-SG neuropeptide (MAB-beta-NP)); Pheromone biosynthesis activating neuropeptide (M); PBAN-type neuropeptides (e.g., Diapause hormone (DH); Alpha-SG neuropeptide (Alpha-SGNP); Beta-SG neuropeptide (Beta-SGNP); Pheromone biosynthesis activating neuropeptide I (PBAN-I) (BoM)); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7) (Fragment); neuropeptides [similarity]; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)); Pol-RFamide neuropeptides; Antho-RFamide neuropeptides type 1; LWamide neuropeptides (e.g., LWamide I; Metamorphosin A (LWamide II) (MMA); LWamide III; LWamide IV; LWamide V; LWamide VI; LWamide VII; LWamide VIII; LWamide IX); Antho-RFamide neuropeptides type 2; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWS); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)]; FMRFamide-like neuropeptides); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (AgI-PBAN); Gamma-SG neuropeptide; FMRFamide-related neuropeptides; Myomodulin neuropeptides (e.g., GLQMLRL-amide; QIPMLRL-amide; SMSMLRL-amide; SLSMLRL-amide; Myomodulin A (PMSMLRL-amide)); FMRFamide neuropeptides; neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWamide III; LWamide IV; LWamide V; LWamide VI; Metamorphosin A (MMA); Mwamide) (Fragment); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (HeA-PBAN); Gamma-SG neuropeptide; Antho-RFamide neuropeptides; Neuropeptides capa receptor (Cap2b receptor); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); FMRFamide-like neuropeptides [e.g., Neuropeptide AF 10 (GFGDEMSMPGVLRF-amide); Neuropeptide AF20 (GMPGVLRF-amide); Neuropeptide AF3 (AVPGVLRF-amide); Neuropeptide AF4 (GDVPGVLRF-amide); N PBAN-type neuropeptides [e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide; Pheromone biosynthesis activating neuropeptide (HeZ-PBAN); Gamma-SG neuropeptide; FMRFamide neuropeptides type FMRF-1 (Fragment); Abdominal ganglion neuropeptides L5-67 (e.g., Luqin; Luqin-B; Luqin-C; Proline-rich mature peptide (PRMP)); FMRFamide neuropeptides type FMRF-2; FMRFamide neuropeptides type FMRF-4 (Fragment); Myomodulin neuropeptides (e.g., Myomodulin A (MM-A) (PMSMLRL-amide) (Neuron B16 peptide); Myomodulin B (MM-B) (GSYRMMRL-amide); Myomodulin D (MM-D) (GLSMLRL-amide); Myomodulin F (MM-F); LWamide neuropeptides (e.g., LWamide I; LWamide II; Metamorphosin A (MMA); Iwamide) (Fragment) (Substance P, calcitonin gene-regulated peptide, and neuropeptide Y.)
E. Other Components
The trophic factor combinations can be used with various delivery systems. In some embodiments, the trophic factor combination is mixed with a viscous substance to increase the viscosity of the combination. The increased viscosity retains the trophic factor combination at the site of the injury longer than it would be retained in the absence of the viscous substance. The viscous substance can be, for example, a polysaccharide, such as hyaluranic acid.
In another embodiment, the trophic factor combination is delivered in a slow release formula, such as in a matrix, for example, a woundhealing matrix, either with or without a viscous substance. In an embodiment, the matrix is a hydrogel, such as a hydrogel disclosed in U.S. Patent Application No. US 20030083389A1, which describes hydrogels wherein a polymer matrix is modified to contain a bifunctional poly(alkylene glycol) molecule covalently bonded to the polymer matrix. The hydrogels can be cross-linked using, for example, glutaraldehyde. The hydrogels can also be crosslinked via an interpenetrating network of a photopolymerizable acrylates. In one embodiment of the invention, the components of the trophic factor combination are incorporated into the hydrogel, for example, through covalent bonds to poly(alkylene glycol) molecules of the hydrogel or through entrainment within the hydrogel. In other embodiments, the matrix is a collagen gel matrix, which can be impregnated with a trophic factor combination. Other matrices can also be used.
The trophic factor combination can also be delivered in a base solution, such as UW solution (DuPont Critical Care, Waukegan, Ill.), or other base solutions.
The neurochemical combinations can be used in conjunction with cell therapy, where transfected cells are produced to release the ingredients and obtain continual delivery of a trophic factor combination. For example, embryonic or adult stem cells can be modified to express trophic factors, antimicrobial peptides, and other relevant neurochemicals, to deliver the trophic factor combination endogenously to the injured spinal cord. In the case of genetically modified cell transplants, the transfected cells can be tagged with cell surface antigens so that the cells can be controlled. For example, antibodies targeting the specific antigen could be used to kill the implanted cells after therapeutic results have been achieved.
Delivery of the neurochemical combinations can also be achieved by media with spaced supports, such as sponges, gels, or biopolymers.
F. Exemplary Formulations
A trophic factor combination includes one or more antimicrobial peptide and/or one or more substance having an antimicrobial peptide effect, alone or with one or more of the following trophic factors: growth factors, neuropeptides, and neurotrophins. Another trophic factor combination includes a viscous substance, such as hyaluronic acid, among others. Another trophic factor combination includes other cytoactive compounds, such as one or more cytokine and/or one or more chemokine. Non-limiting examples of these trophic factor combinations are provided in Tables 3a-3h below. It will be recognized that the trophic factor combinations can comprise one or more antimicrobial polypeptides (e.g., a defensin such as BNP-1). The trophic factor combinations described below can also comprise one or more trophic factors above. Accordingly, in some preferred embodiments, the trophic factor combination is supplemented with one or more of the following trophic factors: trehalose (Sigma, St. Louis Mo.; e.g., about 15 mM), substance P (Sigma; e.g., about 10 μg/ml), IGF-1 (Collaborative Biologicals; e.g., about 10 ng/ml), EGF (Sigma; e.g., about 10 ng/ml), and BDNF (2 μg/ml). In some preferred embodiments, the trophic factor combination is also supplemented with insulin (1-200 units, preferably 40 units) prior to use. In some embodiments, an antimicrobial polypeptide is not included in the trophic factor combination.
In some exemplary embodiments, EGF and/or IGF-1 are included in the trophic factor combination at a concentration of about 1 ng/ml to about 100 ng/ml, most preferably about 10 ng/ml. In other exemplary embodiments, substance P is included at a concentration of about 0.1 μg/ml to about 100 μg/ml, most preferably about 2.5 μg/ml.
It will be recognized that the Tables below provide formulations that are exemplary and non-limiting. For example, alterations in the specific substances used and the number of those substances are all within the scope of the invention. In some embodiments, the antimicrobial polypeptide and/or substance having an antimicrobial peptide effect and/or one or more trophic factor, are provided in stable form that can be reconstituted. Methods for stabilization include, for example, lyophilization. In embodiments where the antimicrobial polypeptide and/or one or more growth factors are provided in lyophilized form, they can conveniently reconstituted prior to use, for example, in sterile water or in an aliquot of a base medium (e.g., UW solution), prior to addition to a base medium (e.g., hyaluronic acid, UW solution).
Alternatively, the at least one microbial polypeptide and/or one or more trophic factor can be provided as a separate composition (i.e., a “bullet”) that is added to a base medium. In preferred embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more trophic factor as described above. In some embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more of the trophic factor as described above in concentrations that provide the appropriate concentration when added to a specific volume of the base medium, where used. TABLE 3a
Component Type Substance
Antimicrobial peptide BNP-1
TABLE 3b
Component Type Substance
Antimicrobial peptide BNP-1
Growth factor IGF-1
TABLE 3c
Component Type Substance
Antimicrobial peptide BNP-1
Neuropeptide Substance P
TABLE 3d
Component Type Substance
Antimicrobial peptide BNP-1
Neurotrophin BDNF
TABLE 3e
Component Type Substance
Antimicrobial peptide BNP-1
Growth factor IGF-1
Neuropeptide Substance P
TABLE 3f
Component Type Substance
Antimicrobial peptide BNP-1
Growth factor IGF-1
Neurotrophin BDNF
TABLE 3g
Component Type Substance
Antimicrobial peptide BNP-1
Neuropeptide Substance P
Neurotrophin BDNF
TABLE 3h
Component Type Substance
Antimicrobial peptide BNP-1
Growth factor IGF-1
Neuropeptide Substance P
Neurotrophin BDNF
It is contemplated that the trophic factor combination can be provided in a pre-formulated form, such as in a kit format. The kit can include (1) at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect and (2) a neurotrophin. The kit can also include a viscous substance. At least one of a growth factor and a neuropeptide can also be included.
II. Uses of Trophic Factor Combinations and Their Individual Components
It is contemplated that the trophic factor combinations and their individual components described above may be utilized in a variety of procedures related to injury to the nervous system and other medical procedures. It is contemplated that the trophic factor combinations and their individual components can be used for the treatment of any part of the nervous system, including the central nervous system and the peripheral nervous system.
In one embodiment, the trophic factor combinations or one or more of their individual components are used during surgery of the disc and/or other portions of the nervous system. In an embodiment, a trophic factor combination or one or more of their individual components applied to surgical hardware and/or other implants, such as surgical screws, plates, pins, clamps, wires, pins, rods, nails, probes, spinal fixation devices, and the like. In another embodiment, a trophic factor combination or one or more of their individual components is applied directly during surgery, such as to a surgical opening, for example, an incision, a section, or any other opening. In one embodiment, a trophic factor combination or one or more of their individual components is applied to one or more tissue, nerve, organ, or cavity. A trophic factor combination or one or more of their individual components can also be applied to a surgical instrument such that when the instrument is used, the trophic factor combination or one or more of their individual components is delivered to injury and/or surrounding tissue, fluid, organ, and the like.
In use, an injury to the nervous system is identified. At least one component of the trophic factor combination is applied to the injury to the nervous system.
In some embodiments, the trophic factor combinations can be utilized to reduce body weight loss post injury in injured animals treated with the combination when compared to injured animals not treated with the trophic factor combination. Preferably, the decrease in loss of body weight is improved by at least 25% and more preferably by at least 50% as compared to animals not receiving the trophic factor combination. In some embodiments, the trophic factor combinations are used to strengthen motor recovery in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to increase evoked potential amplitudes in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to lower the current required to evoke a response (threshold current) in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. Application of the trophic factor combination according to the invention can also have at least one of the following additional effects: reduced pain in the animal, a neuroprotective effect, triggered neuronal plasticity, reduced inflammation, and growth of new cells.
EXAMPLES The following examples serve to illustrate certain preferred embodiments and aspects of the present invention and are not to be construed as limiting the scope thereof.
Example 1 Materials and Methods
Experiments were performed on 3-5 month old male Sprague-Dawley (SD) and Lewis rats that were housed individually with free access to food and water. Rats were placed into four groups: 1) spinally injured SD rats without a trophic factor combination administered (n=8), 2) spinally injured SD rats with a trophic factor combination (n=2); 3) spinally injured Lewis rats without a trophic factor combination administered (n=5), and 4) spinally injured Lewis rats with a trophic factor combination administered (n=2).
Spinal cord injury. Rats were anesthetized with medetomidine (75 μg/kg i.m.) and isoflurane in oxygen. After oro-tracheal intubation, anesthesia was maintained with isoflurane in oxygen and rats were mechanically ventilated. A laminectomy was made at the second cervical vertebral level to allow the second cervical spinal segment and the cranial segment of the third cervical spinal segment to be exposed. A 1-mm-long left-sided hemisection was made in the cranial segment of C2 and the section aspirated with a fine tipped glass pipette. The surgical wound was closed using standard techniques. All animals were allowed to recover and received atipamezole (0.1 mg/kg i.v.) to antagonize the anesthetic effects of medetomidine. Buprenorphine (50 μg/kg i.v.) and carprofen (5 mg/kg i.v.) were administered for postsurgical pain control. Analgesics were repeated as required over the next 2 days.
Trophic Factor Combination. The trophic factor combination (also referred to as the trophic factor combination) was made by adding 10 ug of BNP-1 (bactenecin), 100 ng of insulin-like growth factor (IGF-1), and 25 mg of Substance P to 200 ul of distilled water.
Trophic factor combination administration. Prior to closure of the surgical wound, hyaluronic acid (Hylartin V, sodium hyalurate) (10%) was added to the neurotrophin mixture to thicken the solution and improve retention at the site of spinal injury. Two ug of BDNF was added to 0.4-0.45 ml of the mixture. The mixture (0.4-0.45 ml) was then administered using a syringe and 22-gauge needle into the hemisection cavity. The wound was closed immediately after injection.
Experimental preparation. Two weeks after surgical spinal injury, respiratory motor output was measured from both phrenic nerves using two distinct experimental techniques. First, spontaneous (brain-stem driven) phrenic motor activity was measured in anesthetized rats during standardized conditions. Second, spontaneous activity was removed by hyperventilating the rats and evoke potentials were elicited by spinal stimulation to evaluate the strength of the spinal pathways contributing to motor recovery.
Isoflurane anesthesia was induced in a closed chamber and maintained (2.5-3.5%) via nose cone while rats were tracheotomized. Rats were mechanically ventilated following tracheal cannulation. Following femoral venous catheterization rats were converted to urethane anesthesia (1.6 g/kg) then bilaterally vagotomized and paralyzed with pancuronium bromide (2.5 mg/kg, i.v.). Blood pressure was monitored via a femoral arterial catheter and pressure transducer (Gould P231D, Valley View, Ohio). End-tidal CO2 was monitored with a rapidly responding analyzer (Novametrix, Wallingford, Conn.). Arterial partial pressures of O2 (PaO2) and CO2 (PaCO2) as well as pH were determined from 0.2 ml blood samples (ABL-500, Radiometer, Copenhagen, Denmark); unused blood was returned to the animal. Rectal temperature was maintained (37-39° C.) with a heated table. Phrenic nerves were isolated with a dorsal approach, cut distally, desheathed, bathed in mineral oil and placed on bipolar silver electrodes. Nerve activity was amplified (1000-10,000×) and filtered (100-10,000 Hz bandpass; model 1800, A-M Systems, Carlsborg, Wash.).
Spontaneous phrenic motor output. In all rats, the CO2 apneic threshold for inspiratory activity in the phrenic nerve contralateral to hemisection was determined after waiting a minimum of one hour following conversion to urethane anesthesia. This delay allowed blood pressure and respiratory motor output to stabilize. The procedure to establish the apneic threshold began by increasing the ventilator frequency until inspiratory activity ceased. Ventilator rate was then decreased slowly until inspiratory activity re-appeared. The end-tidal CO2 partial pressure (PETCO2) corresponding to the onset of inspiratory bursting was defined as the CO2 apneic threshold. PETCO2 was maintained 3 mmHg above the apneic threshold by adjusting the ventilator pump rate and inspired CO2 content. After the CO2 apneic threshold and baseline PaCO2 levels were established, 30-45 minutes were allowed to attain stable baseline conditions.
Evoked phrenic potentials. Rats were hyperventilated (PaCO2<30 mmHg) to prevent spontaneous inspiratory efforts. A monopolar tungsten electrode (5 MΩ, A-M Systems) was inserted contralateral to the spinal hemisection and adjacent to the C2 dorsal roots. The electrode tip was placed in or in close proximity to the ventrolateral funiculus (1.8-2.3 mm below the dorsal root entry zone). Electrode position was selected by maximizing the amplitude of a short latency (<1.0 ms) evoked potential in the phrenic nerve contralateral to SCI. Stimulus-response relationships were obtained by applying current pulses (20-1000 μA, 0.2 ms duration) with a stimulator (model S88, Grass Instruments, Quincy, Mass.) and stimulus isolation unit (model PSIU6E, Grass Instruments). Phrenic potentials were digitized and analyzed with P-CLAMP software (Axon Instruments, Foster City, Calif.).
Results:
Body Weight. Body weight decreased by 2 weeks post-injury in rats that had received a spinal hemisection (FIG. 1). Decreased body mass may represent disuse atrophy of skeletal muscles or inadequate caloric intake. Reduced food consumption may occur secondary to spinal cord injury because of motor paresis, reduced locomotor coordination, and/or decreased appetite. Spinally injured rats that received the trophic factor combination had significantly less reduction in body weight compared to the control group (FIG. 1).
Spontaneous Phrenic Nerve Activity. Spontaneous recovery of phrenic motor function on the injured side was evident as inspiratory bursts that were in synchrony with phrenic motor activity on the uninjured side. Phrenic motor recovery was present in all spinally injured rats regardless of treatment. However, the magnitude of this recovery differed between groups (FIG. 2). Administration of the trophic factor combination at the time of injury strengthened motor recovery at 2 weeks post-injury as evident by the significantly larger peak inspiratory voltage during baseline recording conditions (FIG. 2). Phrenic peak inspiratory voltage is correlated to tidal volume. Although tidal volume was not measured in these rats, it is reasonable to assume that the increased peak inspiratory voltage would translate to larger tidal volumes in these animals compared to spinally injured rats that did not receive the trophic factor combination.
Evoked Phrenic Nerve Potentials. Evoked potentials were recorded from the phrenic nerve on the side of injury (FIG. 3). Consistent with the effects of treatment on spontaneous phrenic nerve activity data, administration of trophic factor combination at the time of injury significantly increased evoked potential amplitudes compared to rats that only received a spinal injury.
In addition, a strong trend existed for the current required to evoke a response (threshold current) to be lower after trophic factor combination administration compared to the control group (FIG. 4). Collectively, these data suggest that the trophic factor combination strengthens motor recovery via a spinal mechanism that strengthens existing synaptic pathways onto phrenic motoneurons.
Example 2 This study was performed to determine whether application of a trophic factor combination can improve motor function after spinal cord injury (SCI). In this study, the trophic factor combination of Example 1 was applied and included insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P. The trophic factor combination was applied to test whether this combination would augment spontaneous respiratory motor recovery in a well-defined model of high cervical incomplete spinal cord injury (C2 hemisection). The trophic factor combination was applied to the injured spinal cord at the time of surgical injury. At 2 weeks post-injury, respiratory motor output was recorded bilaterally from phrenic nerves in urethane anesthetized, vagotomized, and mechanically ventilated spinally injured Lewis male rats (SCI-only: n=6; SCI+ trophic factor combination; n=6, with some of these rats being the same as the rats in Example 1). Body weight decreased in all rats after injury. However, the change in body weight was significantly less after trophic factor combination treatment (see FIG. 5; p<0.05). Spontaneous recovery of phrenic motor output on the side of injury was present in all rats and represents activation of a latent population of bulbospinal premotor synaptic pathways to ipsilateral phrenic motoneurons that cross the spinal midline caudal to injury. The trophic factor combination increased the amplitude of phrenic inspiratory bursts on the injured side when measured as rectified and moving-averaged voltages and indexed to the maximal amplitude during hypercapnia (see FIG. 5; p<0.05). In contrast, the trophic factor combination did not alter phrenic motor output on the side opposite injury. Thus, combined treatment with the trophic factor combination improves phrenic motor recovery after C2 hemisection by selectively augmenting crossed spinal synaptic pathways.
Example 3 Subtractive studies. Experiments can be performed on rats in accordance with the methods described in Example 2 except that fewer than all four components, i.e., insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P, of the trophic factor combination can be used (except for one or more controls using all four components). Different components can also be used. For example, a different growth factor (and/or neurotrophin and/or neuropeptide and/or antimicrobial peptide) can be used than the one listed above. Studies can also be run using only one component, i.e., either IGF-1, BDNF, BNP-1, or substance P or any other trophic factor to determine the effects of the individual components. Studies can also be performed using combinations of two of the components and using combinations of three of the components to determine whether all four components are needed to achieve the desired results.
Example 4 Experiments can be performed on dogs having herniated discs. Traditionally, many dogs undergo surgical treatment of disc herniation, but no trophic factor combination has been administered during such surgery. Four naïve dogs can be first treated to test for unanticipated common severe negative effects of the trophic factor combination. Once this is done, 50 dogs presenting to the Veterinary Medical Teaching Hospital (VTMH) at the University of Wisconsin with severe spinal cord dysfunction can be tested.
Trophic factor combination. The trophic factor combination can be formulated of insulin like growth factor-1 (IGF-1) (10 ng/ml), substance P (2.5 μg/ml), bactenecin (1 μg/ml) and brain derived neurotrophic factor (BDNF) (2 μg/ml). The factors can be dissolved in a 1% hyaluronic acid solution. The hyaluronic acid is used in order to increase the contact time of the factors with the tissues.
Dogs that are clinical patients. Surgery can be performed under general anesthesia. A hemilaminectomy can be done at the site of the disc herniation. A 22-gauge catheter can be placed through the dura mater and arachnoid membrane and inserted in the subarachnoid space just caudal to the disc herniation. One ml of the trophic factor combination can be injected in the subarachnoid space. The surgery site can be closed routinely.
After recovery from anesthesia, intravenous lactated Ringer's solution and analgesics can be continued until the dog is able to drink on its own and does not appear painful. Neurologic examinations can be done twice a day. The dogs can be discharged to the owner when they are considered not to need pain medication, can urinate on their own, and are eating and drinking. Follow up examinations can be scheduled as appropriate clinically.
Pain or discomfort during surgery can be alleviated by maintenance of a surgical plane of anesthesia and constant rate infusion (CRI) of fentanyl 10 μg/kg/hr. The fentanyl CRI can be continued up to 12 hours post operatively at a dose of 2-5 μg/kg/hr. A Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours) can be administered as a routine postoperative treatment. Butorphanol can be further administered if the dogs demonstrate discomfort and can be given as long as clinical signs of pain, as indicated by abnormal posturing, vocalization, or discomfort upon palpation of the surgical wound site are present.
Immediately after surgery, the dogs can be monitored continuously until the animals are able to drink water on their own sufficient to maintain their hydration. After this recovery period, the animals can be checked a minimum of 3 times daily to determine if they are experiencing pain or discomfort. The dogs can be evaluated by physical exam, neurological exam, and direct palpation of the surgical wound. The dogs can receive routine recumbent care.
Dogs can be monitored post-surgically for cardiovascular stability by physical exam, pulse character, capillary refill time, heart rate, respiratory rate, and packed cell volume, if needed. Fluids can be administered if needed to maintain hydration. Postoperative discomfort can be alleviated by administration of fentanyl CRI (10 μg/kg/hr) during surgery and fentanyl CRI (2-5 μg/kg/hr) after surgery or butorphanol (0.2-0.4 mg/kg/IV or SQ) every 4-6 hours thereafter and a Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours).
Example 5 Safety trial of trophic factor combination on dogs. The toxicity of the trophic factor combination described in Example 4 was tested on dogs. Four beagle dogs were studied over a three-day period. While the dogs were anesthetized, the trophic factor combination described in Example 4 in hyaluronic acid was injected into 1) the lumbar cerebrospinal fluid (2 dogs) and 2) the cisterna magna cerebrospinal fluid (2 dogs). In all four cases, the dogs recovered easily and showed no signs of toxic reactions. There was no evidence for chronic pain on neurological exam. All dogs were euthanized on the third day of the study. In summary, no adverse reactions were observed in any animal.
It is understood that the various preferred embodiments are shown and described above to illustrate different possible features of the invention and the varying ways in which these features may be combined. Apart from combining the different features of the above embodiments in varying ways, other modifications are also considered to be within the scope of the invention.
The invention is not intended to be limited to the preferred embodiments described above, but rather is intended to be limited only by the claims set out below. Thus, the invention encompasses all alternate embodiments that fall literally or equivalently within the scope of these claims.
