Decoralin, a novel linear cationic α-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus

0301 basic medicine 1303 Biochemistry antimicrobial and leishmanicidal Wasps 2804 Cellular and Molecular Neuroscience amphipathic alpha-helix structure Wasp Venoms Cationic linear α-helical peptide In Vitro Techniques Hemolysis solitary wasp venom Cell Degranulation Protein Structure, Secondary Antimicrobial and leishmanicidal activity Mice 03 medical and health sciences Animals Humans Solitary wasp venom Amino Acid Sequence Mast Cells decoralin Bacteria activity Circular Dichroism 1314 Physiology 540 1310 Endocrinology cationic linear alpha-helical peptide Rats Decoralin Amphipathic α-helix structure Oligopeptides Antimicrobial Cationic Peptides
DOI: 10.1016/j.peptides.2007.09.017 Publication Date: 2007-10-02T07:31:00Z
ABSTRACT
A novel peptide, decoralin, was isolated from the venom of the solitary eumenine wasp Oreumenes decoratus. Its sequence, Ser-Leu-Leu-Ser-Leu-Ile-Arg-Lys-Leu-Ile-Thr, was determined by Edman degradation and corroborated by solid-phase synthesis. This sequence has the characteristic features of linear cationic alpha-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic alpha-helix secondary structure. In fact, the CD spectra of decoralin in the presence of TFE or SDS showed a high alpha-helical conformation content. In a biological evaluation, decoralin exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. A synthetic analog with C-terminal amidation showed a much more potent activity in all the biological assays.
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