Abstract: An instrument and method for accelerating the solid phase synthesis of peptides are disclosed. The method includes the steps of deprotecting a protected first amino acid linked to a solid phase resin by admixing the protected linked acid with a deprotecting solution in a microwave transparent vessel while irradiating the admixed acid and solution with microwaves, activating a second amino acid, coupling the second amino acid to the first acid while irradiating the composition in the same vessel with microwaves, and cleaving the linked peptide from the solid phase resin by admixing the linked peptide with a cleaving composition in the same vessel while irradiating the composition with microwaves.

Abstract: There are provided poly(vinyl alcohol) polymers and copolymers containing vinyl alcohol or vinyl acetate and derivatives thereof such as poly(ethylene glycol)-grafted poly(vinyl alcohol) polymers or polyether-grafted poly(vinyl alcohol) polymers. These polymers can contain various functional groups. Such polymers can be use as polymer matrix or solid support for various chemical substrates such as organic substrates and reagents. Cross-linked poly(vinyl alcohol) polymers and copolymers are also provided. Methods for preparing such polymers as well as several of their uses are also included.

Abstract: The present invention relates to synthetic peptides having selectively protected amines of untargeted sites and to methods for production thereof and for specifically conjugating PEG to targeted sites of the synthetic peptides using the same. The present invention provides a much higher yield of PEG conjugated peptides in which PEG is specifically combined to amines at targeted sites.

Abstract: A method for synthesizing a given peptide or its derivative which contains a proline residue or a proline derivative, at proximity to, or at, the C-terminal end of said peptide is provided. The method comprises a) synthesizing on a first resin a C-terminal portion of said peptide, or its derivative, comprising at least three successive amino acid residues or their derivatives, by successive coupling of selected amino acids, small peptides or their derivatives; b) cleaving the C-terminal portion from said first resin; c) reattaching said C-terminal portion to a second resin which is generally suitable for the synthesis of peptides but is unsuitable for the formation of peptides having a proline residue positioned at the C-terminal end of said peptide; and d) coupling selected amino acids, small peptides or derivatives to the C-terminal portion.

Abstract: A method is presented for the preparation and use of fluorogenic peptide substrates that allows for the configuration of general substrate libraries to rapidly identify the primary and extended specificity of enzymes, such as proteases. The substrates contain a fluorogenic-leaving group, such as 7-amino-4-carbamoylmethyl-coumarin (ACC). Substrates incorporating the ACC leaving group show comparable kinetic profiles as those with the traditionally used 7-amino-4-methyl-coumarin (AMC) leaving group. The bifunctional nature of ACC allows for the efficient production of single substrates and substrate libraries using solid-phase synthesis techniques.

Abstract: A group of new synthetic antimicrobial peptides are disclosed, which demonstrate stronger bactericidal activity than native antimicrobial peptides. The present synthetic antimicrobial peptides can be produced by solid-phase chemical synthesis or gene expression and be used to prepare the medicines for treating the diseases induced by bacteria, viruses and fungi, as well as the anticancer drugs.

Abstract: The invention concerns a peptide based on biologically active CCK-8.

Abstract: Microarrays of polypeptides on a solid support are provided. The microarray compositions find use in the multiplexed detection and quantitation of ligands, e.g. antigens or antibodies, in a miniaturized format. The substrate is used for detecting binding of ligands to a plurality of polypeptides for screening and diagnostic purposes.

Abstract: The present invention is directed to a method for ?N-methylation of amino acids suitable for on-resin methylation, compatible with Fmoc/tBu SPPS, and compatible with amino acids bearing protected or unprotected nucleophilic side-chains, notably Arg(Pbf), Met, Cys, and Trp. The present invention is further directed to a compound of Formula I wherein m, n, X and Y are defined as described herein.

Abstract: Pharmaceutical batch(es) or pharmaceutical formulation(s) comprising bivalirudin as the active ingredient, and a method of preparing the pharmaceutical batch(es) or pharmaceutical formulation(s). The pharmaceutical batch(es) or pharmaceutical formulation(s) may have a maximum impurity level of Asp9-bivalirudin that does not exceed about 0.6%. Also, the pharmaceutical batch(es) or pharmaceutical formulation(s) may have a reconstitution time that does not exceed about 42 seconds. The method of preparing the pharmaceutical batch(es) or pharmaceutical formulation(s) may comprise dissolving bivalirudin in a solvent to form a first solution, efficiently mixing a pH-adjusting solution with the first solution to form a second solution in which the pH-adjusting solution may comprise a pH-adjusting solution solvent, and removing the solvent and the pH-adjusting solution solvent from the second solution.

Abstract: Glycopeptide having at least one asparagine-linked oligosaccharide at a desired position of the peptide chain obtained by: (1) esterifying hydroxyl of a resin and carboxyl of ah amino acid having amino group nitrogen protected with a fat-soluble protective group (AGFPG), (2) removing the protective group to form a free amino group, (3) amidating the free amino group and carboxyl of an amino acid having AGFPG, (4) removing the protective group, (5) repeating the steps (3) and (4), (6) amidating the free amino group and carboxyl of the asparagine portion of an asparagine-linked oligosaccharide having AGFPG, (7) removing the protective group, (8) amidating the free amino group and carboxyl of an amino acid having AGFPG, (9) repeating steps (7) and (8), (10) removing the protective group, and (11) cutting off the resin with an acid; glycopeptide obtained by transferring sialic acid or a derivative thereof to the above glycopeptide.

Abstract: The present invention provides a composition and a method for cleaving a peptide from a solid support resin. Hydrochloric acid in an organic water miscible solvent is used to cleave the peptide-resin attachment. Optionally, trifluoroethanol or hexafluoroisopropanol may be added to the cleavage composition to improve results. When using the present cleavage composition, an evaporation or other step to remove carboxylic byproducts is not necessary following the cleavage reaction. After the resin is filtered out of the cleavage mixture, the peptide may be immediately precipitated with water.

Abstract: An instrument and associated method are disclosed for the accelerated synthesis of peptides by the solid phase method. The instrument includes a microwave cavity, a microwave source in communication with the cavity, a column in the cavity formed of a material that is transparent to microwave radiation, a solid phase peptide support resin in the column, respective filters for maintaining the solid phase support resin in the column, a first passageway for adding starting compositions to the column, a second passageway for removing compositions from the column, and a third passageway for circulating compositions from the column into the third passageway and back to the column.

Abstract: Pharmaceutical batch(es) or pharmaceutical formulation(s) comprising bivalirudin as the active ingredient, and a method of preparing the pharmaceutical batch(es) or pharmaceutical formulation(s). The pharmaceutical batch(es) or pharmaceutical formulation(s) may have a maximum impurity level of Asp9-bivalirudin that does not exceed about 0.6%. Also, the pharmaceutical batch(es) or pharmaceutical formulation(s) may have a reconstitution time that does not exceed about 42 seconds. The method of preparing the pharmaceutical batch(es) or pharmaceutical formulation(s) may comprise dissolving bivalirudin in a solvent to form a first solution, efficiently mixing a pH-adjusting solution with the first solution to form a second solution in which the pH-adjusting solution may comprise a pH-adjusting solution solvent, and removing the solvent and the pH-adjusting solution solvent from the second solution.

Abstract: An instrument and method for accelerating the solid phase synthesis of peptides is disclosed. The method includes the steps of deprotecting a protected first amino acid linked to a solid phase resin by admixing the protected linked acid with a deprotecting solution in a microwave transparent vessel while irradiating the admixed acid and solution with microwaves, then activating a second amino acid by adding the second acid and an activating solution to the same vessel while irradiating the vessel with microwaves, then coupling the second amino acid to the first acid while irradiating the composition in the same vessel with microwaves, and cleaving the linked peptide from the solid phase resin by admixing the linked peptide with a cleaving composition in the same vessel while irradiating the composition with microwaves.

Abstract: The present invention provides methods of assembling oligopeptides or polypeptides in a native chemical ligation reaction that eliminates the formation of unwanted side products resulting from the presence of an unprotected acidic C-terminal oligopeptide thioester. An important aspect of the present invention is providing side chain protected acidic C-terminal oligopeptide thioesters. The present invention is useful in methods for chemical synthesis of oligopeptides, polypeptides and proteins and improves the efficiency of native chemical ligation reactions, particularly where aspartyl or glutamyl peptide fragments are used to assemble an oligopeptide, polypeptide or protein product.

Abstract: An instrument and process for accelerating the solid phase synthesis of peptides is disclosed. The method includes the steps of deprotecting a protected first amino acid linked to a solid phase resin by admixing the protected linked acid with a deprotecting solution in a microwave transparent vessel while irradiating the admixed acid and solution with microwaves, then activating a second amino acid by adding the second acid and an activating solution to the same vessel while irradiating the vessel with microwaves, then coupling the second amino acid to the first acid while irradiating the composition in the same vessel with microwaves, and cleaving the linked peptide from the solid phase resin by admixing the linked peptide with a cleaving composition in the same vessel while irradiating the composition with microwaves.

Abstract: This invention is in the field of snake venom and the invention provides two novel snake polypeptides and nucleic acids encoding the same. Also provided are various uses methods and compositions based on the discovery of the novel snake polypeptides and their ability to synergistically inhibit coagulation.

Abstract: The present invention relates to the preparation of insulinotropic peptides that are synthesized using a solid and solution phase (“hybrid”) approach. Generally, the approach includes synthesizing three different peptide intermediate fragments using solid phase chemistry. Solution phase chemistry is then used to add additional amino acid material to one of the fragments. The fragments are then coupled together in the solution phase. The use of a pseudoproline in one of the fragments eases solid phase synthesis of that fragment and also eases subsequent solution phase coupling of this fragment to other fragments. The present invention is very useful for forming insulinotropic peptides such as Exenatide(1-39) and its natural and non-natural counterparts.

Abstract: The present invention provides a process for producing a peptide thioester compound, characterized by comprising: (A) forming a peptide by a solid-phase synthesis method using a resin modified with a linker represented by the formula (1) as a solid phase; (B) cleaving a bond between the solid phase and the peptide with at least one acid selected from dilute hydrochloric acid, dilute sulfuric acid, formic acid, and acetic acid to produce a peptide having a carboxyl group at the C-terminus; and (C) reacting a thiol compound with the peptide at ?100 to 0° C. in the presence of a condensing agent in a solvent: (1) wherein R1 represents C1-4 alkyl group, R2 represents hydrogen atom or C1-4 alkoxy group, and n represents an integer of 1 to 4.

Abstract: The present invention provides compositions and processes for the solid phase synthesis of polypeptides. In particular, the present invention provides solid supports and processes for preparing solid supports for the synthesis of polypeptides.

Abstract: This invention relates to similar compound of glucagon-like peptide 1(glucagon-like peptide-1, GLP-1) secreted by insulinotropic hormone, i.e. shortened glucagon-like peptide 1(sGLP-1) consisting of 26 aminoacids. Its sequence is as follows: His-X1-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys-Glu-Phe-Ile-Ala-Trp-Leu (SEQ ID NO: 2). In comparison with the present GLP-1 and its similar compound, the shortened glucagon-like peptide 1(sGLP-1) in this invention has the following prominent advantages: 1. After reconstruction, the shortened peptide chain has stronger simulation to islet cell captors and stronger insulin secretion stimulation action; 2. the reconstructed simulation sequence can resist dipeptidyl peptidase decomposition by change of the second aminoacid sequence from Ala to Gly or Ser to prolong its half time and enhance drug action; 3. To shorten the peptide chain leads to reduced synthesis cost.

Abstract: The present invention relates to a process for the preparation of a peptide derivative, and more preferably tri-peptide derivatives, of the formula wherein Tos has the meaning of p-toluenesulfonyl.

Abstract: A backbone nitrogen modifying group can prevent aggregation of peptides during peptide synthesis. The modifying group can promote aqueous solubility of the peptides, and be compatible with solid phase peptide synthesis. Methods for making peptides are also described.

Abstract: The present invention relates to the synthesis of a beaded and cross-linked, high loading capacity polymer for solid phase synthesis, purification of reaction mixtures, chromatographic separation procedures, and the like. The invention can thus be used for the isolation of molecular entities having an affinity for the polymer beads or a chemical entity attached thereto. The beaded polymer matrix can be formed by cross-linking an optionally substituted poly(aminoalkylene), under inverse suspension or inverse emulsion polymerisation conditions, with a cross-linking unit of functionality ?2.

Abstract: An instrument and method for accelerating the solid phase synthesis of peptides is disclosed. The method includes the steps of deprotecting a protected first amino acid linked to a solid phase resin by admixing the protected linked acid with a deprotecting solution in a microwave transparent vessel while irradiating the admixed acid and solution with microwaves, then activating a second amino acid by adding the second acid and an activating solution to the same vessel while irradiating the vessel with microwaves, then coupling the second amino acid to the first acid while irradiating the composition in the same vessel with microwaves, and cleaving the linked peptide from the solid phase resin by admixing the linked peptide with a cleaving composition in the same vessel while irradiating the composition with microwaves.

Abstract: The peptide has a sequence of 3 to 30 adjacent amino acids from the amino end of protein SNAP-25 and is useful as neuronal exocytosis inhibitor. The cosmetic and pharmaceutical compositions contain said peptide and optionally one or more peptides from the carboxyl end of SNAP-25. The compositions are suitable for the treatment of facial wrinkles, asymmetry and pathological neuronal exocytosis-mediated pathological disorders and alterations.

Abstract: A method for preparing a crosslinked polymer coated controlled porosity glass (CPG) particle is provided. The method involves mixing CPG particles in a solution comprising polyvinylbenzylchloride and a first solvent at a temperature below 10° C. A second solvent is added and a crosslinking agent is added to the mixture. The first solvent is removed rapidly within 1½ hours of addition of the crosslinking agent. The crosslinking reaction is permitted to proceed and the mixture is then cooled and treated to remove any remaining solvent. The resulting coated CPG particles are washed and dried. Also provided a polymer coated CPG particles using for loading ligand thereon.

Abstract: The present invention relates to the field of diagnostic and therapeutic use of proteins and genes, in particular to the diagnostic and therapeutic use of a secreted human hormone/growth factor, Neublasmin, and use or the gene coding for Neublasmin in the diagnosis and treatment of testicular disorders, in particular diagnosis and treatment of germ cell tumours and infertility. The invention also relates to use of Neublasmin in the treatment of CNS disorders. Neublasmin is expressed at high levels in human adult testicles and in developing mouse testicles from pn 22 and onwards. Expression or Neublasmin is strongly up-regulated in carcinoma in situ. Expression is also seen in foetal and adult brain.

Abstract: The invention relates to methods for the production of polymer carrier materials for solid phase synthesis, particularly for peptide synthesis. (Meth)acrylamide derivatives based on carbon hydrates, which can also contain other protective groups, are polymerized by means of suspension polymerization in an aqueous phase, optionally with the addition of pore-forming additives, and subsequently the protective groups are fully or partially cleaved. It is thus possible to obtain polymer carriers whose morphology (particle size, porosity), degree of cross-linking and swelling capability in aqueous and organic media can be adjusted in a targeted manner and whose reactive groups offer multiple opportunities for the immobilization of anchor groups and protective groups. The hydroxyl groups of the polymer carrier can be activated according to usual methods of solid phase synthesis.

Abstract: Novel peptide dimers are provided that bind and activate the erythropoietin receptor (EPO-R) or otherwise act as an EPO agonist. The novel compounds have a first peptide chain R1 and a second peptide chain R2, wherein R1 and R2 may be the same or different, and are linked through a linking moiety. R1 is approximately 10 to 40 amino acid residues in length and comprises the sequence X3X4X5GPX6TX7X8X9 (SEQ ID NO: 1) wherein X3 is C or Hoc, X4 is R, H, L or W, X5 is M, F, I or nor-leucine (J), X6 is any one of the 20 genetically coded L-amino acids or J, X7 is W, 1-naphthylalanine (B) or 2-naphthylalanine (U), X8 is D, E, I, L or V, and X9 is C or Hoc. Similarly, R2 comprises the sequence X?3X?4X?5GPX?6TX?7X?8X?9 (SEQ IN NO: 2) wherein X?3 is C or Hoc, X?4 is R, H, L or W, X?5 is M, F, I or J, X?6 is any one of the 20 genetically coded L-amino acids or J, X?7 is W, B or U, X8? is D, E, I, L or V, and X?9 is C or Hoc.

Abstract: The invention relates to methods for the preparation of highly purified peptides. The peptides are prepared in high optical purity of at least about 98.5%, and preferably at least about 99%. Specifically, Nesiritide (SEQ. ID NO. 1) having a purity of at least 99% as measured by HPLC and containing about 0.05% to about 0.5% [D-His]-Nesiritide (SEQ. ID NO. 1) as measured by chiral GC/MS.

Abstract: The present invention provides a novel peptide based on CAP11 as well as provides an antibacterial agent, an LPS-cell-binding inhibitor, and a drug such as a bacterial-infection-treating agent or an endotoxin-shock suppressant, each containing the peptide as an active ingredient. The peptide has the following amino acid sequence (SEQ ID NO: 1): X01 X02 X03 X03 X04 X02 X03 X03 X05 X04 X03 X04 X02 X01 X03 X02 X05 X03 (wherein X01 represents a cationic amino acid residue or a polar uncharged amino acid residue, X02 represents a non-polar amino acid residue, X03 represents a cationic amino acid residue, X04 represents a non-polar amino acid residue or a cationic amino acid residue, and X05 represents a non-polar amino acid residue or a polar uncharged amino acid residue). Each of the antibacterial agent, lipopolysaccharide-cell-binding inhibitor, and drug (e.g., bacterial-infection-treating agent or endotoxin-shock suppressant) contains the peptide as an active ingredient.

Abstract: The present invention is related to new fluorescein derivatives, the method for producing such derivatives and their use for the synthesis of fluorogenic peptides and in particular protease substrates and peptide ligands.

Abstract: New and improved compounds for use in radiodiagnostic imaging or radiotherapy having the formula M-N—O—P-G, wherein M is the metal chelator (in the form complexed with a metal radionuclide or not), N—O—P is the linker, and G is the GRP receptor targeting peptide. Methods for imaging a patient and/or providing radiotherapy to a patient using the compounds of the invention are also provided. A method for preparing a diagnostic imaging agent from the compound is further provided. A method for preparing a radiotherapeutic agent is further provided.

Abstract: A process for preparing a peptide or protein by solid phase synthesis comprising combining a sequence including one or more amino acids obtainable by C-N synthesis linked to a first resin, with an amino acid sequence including one or more amino acid obtainable by N-C synthesis linked to a second resin so as to create a native peptide link between unprotected N and unprotected C terminals of said amino acid sequences, and optionally releasing the resulting peptide from one or more of the linked resins so as to combine with further N-C or C-N sequences or to release the desired peptide or protein sequence.

Abstract: Method of making metallopeptides is provided, for use in biological, pharmaceutical and related applications. The metallopeptides are made of peptides, peptidomimetics and peptide-like constructs, and include a metal ion-binding region thereof which includes at least one orthogonal sulfur-protecting group, in which the peptide, peptidomimetic or construct is conformationally fixed on deprotection of the sulfur and complexation of the metal ion-binding region with a metal ion while the peptide, peptidomimetic or construct is cleavably bound to solid phase.

Abstract: The invention concerns a novel surface-functionalized carrier material with a polymeric surface and at least one linker compound according to the general formula (I), which is covalently bound to the surface. In the formula, P indicates the polymeric surface; R2 has the meaning OR4 or NR4R5 and R1, R4 and R5, independently of one another, indicate H, an alkyl group or an aryl group; R3 indicates H, an alkyl, an aryl, an acyl, an alkoxycarbonyl or an aryloxycarbonyl group; and the alkyl, aryl, acyl, alkoxycarbonyl and/or aryloxycarbonyl group of the radicals R1, R3, R4 and R5, independently of one another, are substituted or unsubstituted. The material according to the invention can be very easily produced by photochemical coupling and serves for the solid-phase synthesis of amino acids, peptides, proteins or molecules with at least one peptidic structural unit.

Abstract: The present invention provides a protein synthesis method for efficiently synthesizing a desired protein so that it is properly folded so as to demonstrate a function thereof, the method comprising contacting a translation system with a solid phase-immobilized mRNA in which mRNA encoding that protein is immobilized on a solid phase, a protein synthesis apparatus for the method or the like. The protein synthesis method, protein synthesis apparatus or the like of the present invention are useful for, for example, large-volume synthesis of useful proteins.

Abstract: Method of peptide synthesis, comprising the steps of a. synthesizing a peptide linked to a solid phase which peptide comprises at least one cysteine, homo- or nor-cysteine residue, which cysteine is protected in its side chain by a S-tert.butyl-sulphenyl group b. either coupling N-terminally a further amino acid having a 3,3?-dithio-(1-carboxy-propyl)-propionyl-radical on its N? or deprotecting the N? of the N-terminal amino acid and reacting the free N? with 3,3?-dithio-propionic acid imide to yield the corresponding N?-3,3?-dithio-(1-carboxy-propyl)-propionamide or deprotecting the N? of the N-terminal amino acid and reacting the free N? with a compound of formula IV R7-S—S—[CH2]2—COOH IV wherein R7 is aryl-, including heteronuclear aryl, or is aralkyl-, alkylaryl- or alkyl-, which may be further substituted with halogeno, amido, ester, carboxy or ether, and c. reacting the peptide with a S-tert.Butyl-sulphenyl-protection group removing reagent, and d.

Abstract: The invention is directed to a pharmacologically active peptide conjugate having a reduced tendency towards enzymatic cleavage comprising a pharmacologically active peptide sequence (X) and a stabilizing peptide sequence (Z) of 4-20 amino acid residues covalently bound to X.

Abstract: Disclosed herein is a new method for the solid phase peptide synthesis (SPPS) of C-terminal peptide ? thioesters using Fmoc/t-Bu chemistry. This method is based on the use of an aryl hydrazine linker, which is totally stable to conditions required for Fmoc-SPPS. When the peptide synthesis has been completed, activation of the linker is achieved by mild oxidation. The oxidation step converts the acyl-hydrazine group into a highly reactive acyl-diazene intermediate which reacts with an ?-amino acid alkylthioester (H-AA-SR) to yield the corresponding peptide ?-thioester in good yield. A variety of peptide thioesters, cyclic peptides and a fully functional Src homology 3 (SH3) protein domain have been successfully prepared.

Abstract: Molecules having potential biological activity, particularly peptoids, that are conjugated to solid phase supports, spacer groups, and/or ligation moieties, and methods of their preparation, are described. In some instances, the molecules of the invention are made entirely by solid phase synthesis. In other instances, the spacer groups are hydrophilic and compositions containing them, and to solid phase synthesis of varied structure peptoids using chemoselective ligation moieties.

Abstract: A novel method for side chain cyclisation of peptides by means of lactamization is provided.

Abstract: The present invention relates to novel anti-hypertensive molecules. The present invention also provides a process for the preparation of novel antihypertensive molecules. The present invention particularly relates to the preparation of novel Angiotensin Converting Enzyme Inhibitors (ACEI) with prolonged activity. ACE inhibitors play an important role in Re -Angiotensin-Aldosteron system (RAAS) by inhibiting the activity of Angiotensin Converting Enzyme (ACE) and therefore are used to regulate blood pressure. ACE inhibitors synthesized by the process of present invention have a peptide moiety and nonpeptide moiety. ACE inhibitors, synthesized by this present invention, show enhanced bioavailability and fewer side effects.

Abstract: The present invention is directed to a method for synthesizing a peptide using solid-state chemistry in which at least one amide bond is N-methylated, wherein said method of synthesis utilizes N-Boc protected amino acids. For example, the a peptide is first synthesized using N-BOC protected amino acids and 4-methylbenzylhydrylamine functionalized 1% cross linked polystyrene resin until reaching the amide bond to be N-methylated. Then, the amino group at the desired methylation site is methylated. If desired, the synthesis of additional peptide using N-BOC protected amino acids may continued until the desired peptide is complete.

Abstract: An instrument and process for accelerating the solid phase synthesis of peptides is disclosed. The method includes the steps of deprotecting a protected first amino acid linked to a solid phase resin by admixing the protected linked acid with a deprotecting solution in a microwave transparent vessel while irradiating the admixed acid and solution with microwaves, then activating a second amino acid by adding the second acid and an activating solution to the same vessel while irradiating the vessel with microwaves, then coupling the second amino acid to the first acid while irradiating the composition in the same vessel with microwaves, and cleaving the linked peptide from the solid phase resin by admixing the linked peptide with a cleaving composition in the same vessel while irradiating the composition with microwaves.

Abstract: Metal chelators of formula (I) and formula (II) are disclosed or a farmaceutically acceptable salt thereof. Also disclosed are metal chelator-targeting moiety complexes, metal chelator-targeting moiety-metal conjugates, kits, and methods of their preparation and use in diagnosis and/or treatment of diseases and conditions, including, inter alia, cancer and thrombosis.

Abstract: The instant invention comprises a process for the solid phase synthesis of directed epitope peptide mixtures useful in the modulation of unwanted immune responses, such process defined by a set of rules regarding the identity and the frequency of occurrence of amino acids that substitute a base or native amino acid of a known epitope. The resulting composition is a mixture of related peptides for therapeutic use.

Abstract: The present invention provides methods of selecting and uses of anti-arthropod vector vaccines to prevent Leishmaniasis. The present invention also provides compositions for vaccines to prevent Leishmaniasis.