Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorKonno, K.
dc.creatorHisada, M.
dc.creatorFontana, R.
dc.creatorLorenzi, CCB
dc.creatorNaoki, H.
dc.creatorItagaki, Y.
dc.creatorMiwa, A.
dc.creatorKawai, N.
dc.creatorNakata, Y.
dc.creatorYasuhara, T.
dc.creatorNeto, JR
dc.creatorde Azevedo, W. F.
dc.creatorPalma, Mario Sergio
dc.creatorNakajima, T.
dc.date2014-05-20T15:30:40Z
dc.date2016-10-25T18:06:15Z
dc.date2014-05-20T15:30:40Z
dc.date2016-10-25T18:06:15Z
dc.date2001-11-26
dc.date.accessioned2017-04-06T00:18:17Z
dc.date.available2017-04-06T00:18:17Z
dc.identifierBiochimica Et Biophysica Acta-protein Structure and Molecular Enzymology. Amsterdam: Elsevier B.V., v. 1550, n. 1, p. 70-80, 2001.
dc.identifier0167-4838
dc.identifierhttp://hdl.handle.net/11449/40001
dc.identifierhttp://acervodigital.unesp.br/handle/11449/40001
dc.identifier10.1016/S0167-4838(01)00271-0
dc.identifierWOS:000172738000008
dc.identifierhttp://dx.doi.org/10.1016/S0167-4838(01)00271-0
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/882824
dc.descriptionA novel antimicrobial peptide, anoplin, was purified from the venom of the solitary wasp Anoplius samariensis. The sequence was mostly analyzed by mass spectrometry, which was corroborated by solid-phase synthesis. Anoplin, composed of 10 amino acid residues, Gly-Leu-Leu-Lys-Arg-Ile-Lys-Thr-Leu-Leu-NH2, has a high homology to crabrolin and mastoparan-X, the mast cell degranulating peptides from social wasp venoms, and, therefore, can be predicted to adopt an amphipathic alpha -helix secondary structure. In fact, the circular dichroism. (CD) spectra of anoplin in the presence of trifluoroethanol or sodium dodecyl sulfate showed a high content, up to 55% of the alpha -helical conformation. A modeling study of anoplin based on its homology to mastoparan-X supported the CD results. Biological evaluation using the synthetic peptide revealed that this peptide exhibited potent activity in stimulating degranulation from rat peritoneal mast cells and broad-spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria. Therefore, this is the first antimicrobial component to be found in the solitary wasp venom and it may play a key role in preventing potential infection by microorganisms during prey consumption by their larvae. Moreover, this peptide is the smallest among the linear alpha -helical antimicrobial peptides hitherto found in nature, which is advantageous for chemical manipulation and medical application. (C) 2001 Elsevier B.V. B.V. All rights reserved.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimica Et Biophysica Acta-protein Structure and Molecular Enzymology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectanoplin
dc.subjectantimicrobial peptide
dc.subjectamphipathic alpha-helical structure
dc.subjectsolitary wasp venom
dc.titleAnoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis
dc.typeOtro


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