Abstract: The present invention relates to the field of antimicrobial agents. In particular, the present invention relates to polypeptides comprising the sequence of a peptidoglycan hydrolase and a peptide sequence heterologous to the peptidoglycan hydrolase wherein said heterologous peptide sequence comprises a specific sequence motif which is 16, 17, 18, 19 or 20 amino acids in length. The present invention relates also to corresponding nucleic acids, vectors, bacteriophages, host cells, compositions and kits. The present inventions also relates to the use of said polypeptides, nucleic acids, vectors, bacteriophages, host cells, compositions and kits in methods for treatment of the human or animal body by surgery or therapy or in diagnostic methods practiced on the human or animal body. The polypeptides, nucleic acids, vectors, bacteriophages, host cells, compositions and kits according to the invention may also be used as an antimicrobial in, e.g., food or feed, in cosmetics, or as disinfecting agent.

Abstract: The inventors provide a composition comprising an antimicrobial polypeptide comprising Blad or an active variant thereof for use in a method of treatment of the human or animal body by therapy or prophylaxis, such as for use in a method of treating or preventing an infection in or on a subject by a microorganism. Also provided is the use of a composition comprising an antimicrobial polypeptide comprising Blad or an active variant thereof to kill, or inhibit the growth of, a microorganism that is pathogenic to a human or an animal at a site that is not on or in the human or animal body.

Abstract: The inventors provide the use of a chelating agent and an antimicrobial agent that is effective against a plant pathogenic microorganism to inhibit the growth of and/or kill a plant pathogenic microorganism on a plant; the use of a chelating agent to increase the activity of an antimicrobial that is effective against a plant pathogenic microorganism; a method of inhibiting the growth of and/or killing a plant pathogenic microorganism comprising administering to a plant in need thereof a chelating agent and an antimicrobial agent that is effective against a plant pathogenic microorganism; and a method of increasing the activity of an antimicrobial that is effective against a plant pathogenic microorganism comprising using said antimicrobial with a chelating agent.

Abstract: Novel compounds and methods for the inhibition of biological barrier permeability and for the inhibition of peptide translocation across biological barriers are identified. Assays for determining modulators of biological barrier permeability and for peptide translocation across biological barriers are provided. Methods for treating diseases relating to aberrant biological barrier permeability and peptide translocation across biological barriers are provided. Such diseases include celiac disease, necrotizing enterocolitis, diabetes, cancer, inflammatory bowel diseases, asthma, COPD, excessive or undesirable immune response, gluten sensitivity, gluten allergy, food allergy, rheumatoid arthritis, multiple sclerosis, immune-mediated or type 1 diabetes mellitus, systemic lupus erythematosus, psoriasis, scleroderma and autoimmune thyroid diseases.

Abstract: Disclosed herein are methods and compositions for the treatment and/or prevention of diseases or conditions comprising administration of a therapeutic biological molecule, and/or naturally or artificially occurring derivatives, analogues, or pharmaceutically acceptable salts thereof, alone or in combination with one or more active agents (e.g., an aromatic-cationic peptide). The present technology provides compositions related to aromatic-cationic peptides linked to a therapeutic biological molecule and uses of the same. In some embodiments, the aromatic-cationic peptide comprises 2?,6?-dimethyl-Tyr-D-Arg-Phe-Lys-NH2, Phe-D-Arg-Phe-Lys-NH2, or D-Arg-2?,6?-Dmt-Lys-Phe-NH2.

Abstract: The invention discloses a polypeptide with improved alkaline stability, which polypeptide comprises a mutant of a B or C domain of Staphylococcus Protein A (SpA), as specified by SEQ ID NO 1 or SEQ ID NO 2, or of Protein Z, as specified by SEQ ID NO 3, wherein at least the glutamine residue at position 9 has been mutated to an amino acid other than asparagine. The invention also discloses multimers of said polypeptide, as well as separation matrices comprising the multimers or polypeptides.

Abstract: A kappa light chain-binding polypeptide comprising or consisting essentially of one or more mutated binding domains of Peptostreptococcus Protein L.

Abstract: Disclosed herein are compositions comprising a CT20 peptide and methods of using the disclosed compositions to treat cancers expressing chaperonin containing TCP (CCT).

Abstract: The present invention relates to compounds having activity at both the human glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) receptors. The present invention also relates to compounds having an extended duration of action at each of these receptors. Furthermore, the present invention relates to compounds that may be administered orally. Compounds may be useful in the treatment of type 2 diabetes mellitus (“T2DM”). Also, the compounds may be useful in the treatment of obesity.

Abstract: An example of the composition incudes at least one amino acid sequence from the octarepeat region of hemin that is modified by substituting at least one proline (P) residue in the amino acid sequence. The composition is effective to bind with hemin and for treating hemorrhagic injury.

Abstract: Provided is a novel peptide for skin regeneration or wound healing and a use thereof. The novel peptide not only promotes the wound healing by increasing the production amount of collagen in dermal fibroblasts but also has an excellent whitening effect by inhibiting the production amount of melanin and tyrosinase activity of melanoma cells, and consists of peptides having a very small size to minimize side effects according to administration of external substances of very small peptides. As a result, it is expected that the novel peptide can be used as an active substance that can replace existing skin regeneration or would therapeutic agents.

Abstract: The present invention provides compositions comprising insulin receptor partial agonists in association with GLP-1 analogues (e.g., liraglutide) as well as methods for using the compositions for example, to treat or prevent diabetes or to decrease body weight.

Abstract: An Fc-binding polypeptide of improved alkali stability, comprising a mutant of an Fc-binding domain of Staphylococcus Protein A (SpA), as defined by SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO:3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID NO:8, SEQ ID NO 26 or SEQ ID NO 27, wherein at least the alanine residue at the position corresponding to position 42 in SEQ ID NO:4-7 has been mutated to arginine and/or wherein at least the aspartic acid residue at the position corresponding to position 37 in SEQ ID NO:4-7 has been mutated to glutamic acid.

Abstract: The present invention relates to a bioassimilable protein-melanin complex, advantageously soluble in water, comprising a protein extract, advantageously rich in S-sulfonated residues and melanin. The claimed complex further exhibits subsequent good assimilation in the human body. The invention also relates to a method for preparing the claimed bioassimilable protein-melanin complex, use of said complex and compositions containing at least said complex.

Abstract: Provided is a method for producing a short-chain peptide-immobilized carrier that maintains a secondary structure of a short-chain peptide, the method including a step of preparing an alcohol solution containing an alcohol solvent, and a short-chain peptide having a plurality of immobilizing functional groups, the short-chain peptide having a secondary structure induced in the alcohol solvent; and a step of bringing a carrier coupled with a spacer having a reactive group that reacts with the immobilizing functional group, into contact with the alcohol solution, and thereby immobilizing the short-chain peptide to the spacer.

Abstract: Provided are astexin-1, astexin-2 and astexin-3 lasso peptides, which are based on sequences identified in Asticcacaulis excentricus, and methods of making and using same. Astexin-1 is highly polar, in contrast to many lasso peptides that are primarily hydrophobic, and has modest antimicrobial activity against Caulobacter crescentus, a bacterium related to Asticcacaulis excentricus. The solution structure of astexin-1 was determined, revealing a unique topology that is stabilized by hydrogen bonding between segments of the peptide. Astexins-2 and -3 are intracellular lasso peptides.

Abstract: Methods for purifying a polypeptide from a composition comprising the polypeptide and at least one contaminant are described, which methods comprise the sequential steps of: (a) passing the composition through an ion exchange membrane, where the polypeptide and the membrane have opposite charge, at operating conditions comprised of a buffer having a pH sufficiently distinct from the pI of the polypeptide to enhance the charge of the polypeptide and a low ionic strength effective to prevent the shielding of charges by buffer ions, which cause the membrane to bind the polypeptide and the at least one contaminant, and (b) recovering the purified polypeptide from the effluent.

Abstract: Disclosed are a translationally controlled tumor protein derived-protein transduction domain (TCTP-PTD) having the ability to penetrate the cell membrane, and to the use thereof. The TCTP-PTD peptide is capable of improving the ability of a target substance to penetrate the cell membrane to thereby effectively deliver the target substance into a living body, including cells, tissue and blood. Thus, the TCTP-PTD peptide may be used for research purposes in vitro, and may be used for clinical purposes, including treatment of various diseases, delivery of contrast agents, etc., and may also be used for diagnostic purposes and in cosmetic applications.

Abstract: The present disclosure generally relates to a circularized peptide for treating cancer. An cyclic peptide is disclosed that has an amino acid sequence selected from Lys-X5-Glu-X1-X2-Gln-Met-Glu-Asp-Asp-X3-X4 (SEQ ID NO: 3), (SEQ ID NO: 4), Lys-Gly-X6-Val-Leu-Gln-Met-X7-X8-X9-Leu-Val (SEQ ID NO: 5), Lys-X5-Glu-X1-X2-Gln-X12-Glu-Asp-Asp-X3-X4 (SEQ ID NO: 9), and X10-X5-X6-Val-Leu-Gln-Met-Glu-Asp-X9-X3-X4 (SEQ ID NO: 10). The amino acids X1, X2, X3, and X4 can be each independently valine, leucine, isoleucine, or alanine; X5 can be glycine, alanine, leucine, isoleucine, or valine; X6, X7, X8, and X9 can be each independently glutamic acid or asparagine; X10 can be lysine or arginine; X11 can be methionine or cysteine; and X12 can be methionine or norleucine. The cyclic peptide can have the amino acid sequence Lys-Gly-Glu-Val-Leu-Gln-Met-Glu-Asp-Asp-Leu-Val (SEQ ID NO: 1).

Abstract: Described herein are bioactive peptides that are modified at one or more positions with a PEG moiety. An example of such a PEGylated bioactive peptide is a GHRH analog that is modified at one or more positions with a PEG moiety. Also described are pharmaceutically acceptable salts thereof and pharmaceutical compositions comprising such analogs or salts thereof, as well as methods, kits and uses thereof, for example for inducing or stimulating growth hormone secretion in a subject and for diagnosing, preventing or treating GH-deficient conditions in a subject.