The present invention provides an agent, or a composition containing an agent, for use in treating or preventing a bacterial infection in a subject, wherein said agent comprises: (i) an oligopeptidic compound comprising a PCNA interacting motif and a domain that facilitates the cellular uptake of said compound, wherein the PCNA interacting motif is X.sub.1X.sub.2X.sub.3X.sub.4X.sub.5X.sub.6 (SEQ ID NO: 1) and wherein: X.sub.1 is a basic amino acid; X.sub.2 is an aromatic amino acid; X.sub.3 is an aromatic amino acid or a hydrophobic amino acid that has an R group comprising at least three carbon atoms; X.sub.4 is an uncharged amino acid other than an aromatic amino acid, Glycine (G) and Proline (P); X.sub.5 is any amino acid other than an acidic amino acid or an aromatic amino acid; and X.sub.6 is any amino acid other than an acidic amino acid or an aromatic amino acid, preferably a basic amino acid or Proline (P), wherein when X.sub.3 is not an aromatic amino acid, X.sub.5 is not lysine (K) and X.sub.6 is a basic amino acid or Proline (P); or (ii) a nucleic acid molecule comprising a sequence encoding the oligopeptidic compound of (i). In certain aspects the agent and composition of the invention may be used as single agents. In other aspects of the invention the agents and composition may be used in conjunction with one or more addition active agents, such as antibiotics, or in combination with UV radiation.

Provided are a conotoxin peptide -CPTx-bt103 and a derivative polypeptide. The amino acid sequence of the conotoxin peptide is indicated by SEQ ID NO: 1. Also provided are a conotoxin peptide preparation method and uses of the conotoxin peptide in the treatment of diseases related to a calcium ion channel.

Disclosed are peptides that induce an active plant response, but not a hypersensitive response, when applied to plant tissue. These peptides also preferably exhibit improved solubility, stability, resistance to chemical degradation, or a combination of these properties. Use of these peptides or fusion polypeptides, or DNA constructs encoding the same, for modulating plant biochemical signaling, imparting disease resistance to plants, enhancing plant growth, imparting tolerance to biotic stress, imparting tolerance and resistance to abiotic stress, imparting desiccation resistance to cuttings removed from ornamental plants, imparting post-harvest disease or post-harvest desiccation resistance to a fruit or vegetable, or enhancing the longevity of fruit or vegetable ripeness are also disclosed.

A pentapeptide associated with integrin receptor v3, which has a sequence of arginine-tryptophan-arginine-asparagine-methionine. The pentapeptide targets tumor cells highly expressing v3, but not tumor cells lowly expressing v3 and normal cells. Accordingly, the pentapeptide is useful in the diagnosis and treatment of cancers.

A method of treating a synucleinopathy with a peptide (C)DQPVLPD (SEQ ID NO: 59), (C)DMPVLPD (SEQ ID NO: 60), (C)DSPVLPD (SEQ ID NO: 61), (C)DQPVLPDN (SEQ ID NO: 64), (C)DMPVLPDN (SEQ ID NO: 65), (C)DSPVLPDN (SEQ ID NO: 66), (C)HDRPVTPD (SEQ ID NO: 70), (C)DRPVTPD (SEQ ID NO: 71), (C)DVPVLPD (SEQ ID NO: 72), (C)DTPVYPD (SEQ ID NO: 73), (C)DTPVIPD (SEQ ID NO: 74), (C)HDRPVTPDN (SEQ ID NO: 75), (C)DRPVTPDN (SEQ ID NO: 76), (C)DVPVLPDN (SEQ ID NO: 78), (C)DTPVYPDN (SEQ ID NO: 79), (C)DQPVLPDG (SEQ ID NO: 81), (C)DMPVLPDG (SEQ ID NO: 82), (C)DSPVLPDG (SEQ ID NO: 83), (C)DHPVHPDS (SEQ ID NO: 86), (C)DMPVSPDR (SEQ ID NO: 87), (C)DRPVYPDI (SEQ ID NO: 90), (C)DHPVTPDR (SEQ ID NO: 91), (C)DTPVLPDS (SEQ ID NO: 93), (C)DMPVTPDT (SEQ ID NO: 94), (C)DAPVTPDT (SEQ ID NO: 95), (C)DSPVVPDN (SEQ ID NO: 96), (C)DLPVTPDR (SEQ ID NO: 97), (C)DSPVHPDT (SEQ ID NO: 98), (C)DAPVRPDS (SEQ ID NO: 99), (C)DMPVLPDG (SEQ ID NO: 100), (C)DRPVQPDR (SEQ ID NO: 102), (C)YDRPVQPDR (SEQ ID NO: 103), (C)DMPVDADN (SEQ ID NO: 105), DQPVLPD(C) (SEQ ID NO: 106), and DMPVLPD(C) (SEQ ID NO: 107.

Agents that inhibit the dimerization of a prototypic galectin such as galectin-7 are described. These agents, for example antibodies and peptides, bind to a domain corresponding to residues 13-25, 86-108 and/or 129-135 of human galectin-7. The use of such agents to inhibit a biological, physiological and/or pathological process that involves prototypic galectin dimerization, for example for the inhibition of galectin-7-mediated apoptosis and the treatment of galectin-7-expressing cancers, is also described.

A method of treating or preventing a bacterial infection in an animal comprises administering to the animal an effective amount of an antibacterial peptide, the antibacterial peptide being derived from degraded date pits which are degraded by solid state degradation by a fungus, Trichoderma reesei. The antibacterial peptide has a molecular mass of less than 10 kDa and an amino acid sequence including (a) SEQ ID NO:4 or (b) SEQ ID NO:6. The bacterial infection is caused by a Gram-positive bacteria or a Gram-negative bacteria, for example, a Salmonella species, a Campylobacter species, a Shigella species, an Escherichia species, a Pseudomonas species, and a Staphylococcus species.

A family of peptides with antioxidant and brightening activities is disclosed as well as cosmetic compositions having the peptides and cosmetic uses and methods of the peptides or cosmetic compositions.

A peptide compound having a dipeptidyl peptidase-IV (DPPIV) inhibitory activity or a composition containing the peptide compound that can make a contribution to the prevention of the onset of pathology or the progression in diabetes mellitus patients or those at risk of diabetes mellitus can be provided according to the present invention by a simple method using, as a raw material, milt of a fishery product, which has been eaten for ages and has high safety. In the present invention, a peptide compound having a peptidyl peptidase-IV (DPPIV) inhibitory activity obtained in a hydrolysate of a milt protein source obtained from a fishery product is used as an active component of a composition for inhibiting DPPIV.

The invention describes peptide ligands specific for human plasma Kallikrein.