Journal
PEPTIDES
Volume 28, Issue 12, Pages 2320-2327Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2007.09.017
Keywords
decoralin; solitary wasp venom; cationic linear alpha-helical peptide; amphipathic alpha-helix structure; antimicrobial and leishmanicidal; activity
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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 a-helical peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, it can be predicted to adopt an amphipathic a-helix secondary structure. In fact, the CD spectra of decoralin in the presence of TFE or SDS showed a high a-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. (c) 2007 Elsevier Inc. All rights reserved.
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