Artigo
Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus
Fecha
2007-12-01Registro en:
Peptides. New York: Elsevier B.V., v. 28, n. 12, p. 2320-2327, 2007.
0196-9781
10.1016/j.peptides.2007.09.017
WOS:000251698000009
Autor
Instituto Butantan
Universidade Estadual Paulista (Unesp)
Univ Estadual Santa Cruz
Universidade Federal de São Paulo (UNIFESP)
Hiroshima Univ
Tokushima Bunri Univ
Josai Int Univ
Natl Inst Biomed Innovat
Resumen
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 B.V. All rights reserved.