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

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dc.contributor.authorKonno, Katsuhiro
dc.contributor.authorRangel, Marisa
dc.contributor.authorOliveira, Joacir Stolarz
dc.contributor.authorSantos Cabrera, Marcia Perez Dos [UNESP]
dc.contributor.authorFontana, Renato
dc.contributor.authorHirata, Izaura Yoshico
dc.contributor.authorHide, Lzumi
dc.contributor.authorNakata, Yoshihiro
dc.contributor.authorMori, Kanami
dc.contributor.authorKawano, Marii
dc.contributor.authorFuchino, Hiroyuki
dc.contributor.authorSekita, Setsuko
dc.contributor.authorNeto, Joao Ruggiero
dc.contributor.institutionInstituto Butantan
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Estadual Santa Cruz
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionHiroshima Univ
dc.contributor.institutionTokushima Bunri Univ
dc.contributor.institutionJosai Int Univ
dc.contributor.institutionNatl Inst Biomed Innovat
dc.date.accessioned2014-05-20T15:28:53Z
dc.date.available2014-05-20T15:28:53Z
dc.date.issued2007-12-01
dc.description.abstractA 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.en
dc.description.affiliationInstituto Butantan, Ctr Appl Toxinol, BR-05503900 São Paulo, SP, Brazil
dc.description.affiliationSão Paulo State Univ, Inst Biosci Letters & Exact Sci, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUniv Estadual Santa Cruz, Dept Biol Sci, BR-4565000 Ilheus, BA, Brazil
dc.description.affiliationUniv Fed São Paulo, Paulista Med Sch, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationHiroshima Univ, Grad Sch Biomed Sci, Dept Pharmacol, Hiroshima 7348553, Japan
dc.description.affiliationTokushima Bunri Univ, Fac Pharmaceut Sci, Kagawa 7692193, Japan
dc.description.affiliationJosai Int Univ, Fac Pharmaceut Sci, Chiba 2838555, Japan
dc.description.affiliationNatl Inst Biomed Innovat, Res Ctr Med Plant Resources, Tsukuba, Ibaraki 3050843, Japan
dc.description.affiliationUnespSão Paulo State Univ, Inst Biosci Letters & Exact Sci, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent2320-2327
dc.identifierhttp://dx.doi.org/10.1016/j.peptides.2007.09.017
dc.identifier.citationPeptides. New York: Elsevier B.V., v. 28, n. 12, p. 2320-2327, 2007.
dc.identifier.doi10.1016/j.peptides.2007.09.017
dc.identifier.issn0196-9781
dc.identifier.urihttp://hdl.handle.net/11449/38617
dc.identifier.wosWOS:000251698000009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofPeptides
dc.relation.ispartofjcr2.851
dc.relation.ispartofsjr1,001
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectdecoralinpt
dc.subjectsolitary wasp venompt
dc.subjectcationic linear alpha-helical peptidept
dc.subjectamphipathic alpha-helix structurept
dc.subjectantimicrobial and leishmanicidalpt
dc.subjectactivitypt
dc.titleDecoralin, a novel linear cationic alpha-helical peptide from the venom of the solitary eumenine wasp Oreumenes decoratusen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0001-7443-2883[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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