Decoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratus
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Data
2007-12-01
Autores
Konno, Katsuhiro
Rangel, Marisa
Oliveira, Joacir Stolarz
Santos Cabrera, Marcia Perez Dos [UNESP]
Fontana, Renato
Hirata, Izaura Yoshico
Hide, Lzumi
Nakata, Yoshihiro
Mori, Kanami
Kawano, Marii
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Editor
Elsevier B.V.
Resumo
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.
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decoralin, solitary wasp venom, cationic linear alpha-helical peptide, amphipathic alpha-helix structure, antimicrobial and leishmanicidal, activity
Como citar
Peptides. New York: Elsevier B.V., v. 28, n. 12, p. 2320-2327, 2007.