New mastoparan peptides in the venom of the solitary eumenine wasp eumenes micado

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dc.contributorLab. Imunopatologiapt_BR
dc.contributor.authorKonno, Katsuhiropt_BR
dc.contributor.authorKazuma, Koheipt_BR
dc.contributor.authorRangel, Marisapt_BR
dc.contributor.authorStolarz-de-Oliveira, Joacirpt_BR
dc.contributor.authorFontana, Renatopt_BR
dc.contributor.authorKawano, Mariipt_BR
dc.contributor.authorFuchino, Hiroyukipt_BR
dc.contributor.authorHide, Izumipt_BR
dc.contributor.authorYasuhara, Tadashipt_BR
dc.contributor.authorNakata, Yoshihiropt_BR
dc.date.accessioned2020-07-09T21:23:09Z-
dc.date.available2020-07-09T21:23:09Z-
dc.date.issued2019pt_BR
dc.identifier.citationKonno K, Kazuma K, Rangel M, Stolarz-de-Oliveira J, Fontana R, Kawano M, et al. New mastoparan peptides in the venom of the solitary eumenine wasp eumenes micado. Toxins. 2019 Mar;11(3):155. doi:10.3390/toxins11030155.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2688-
dc.description.abstractComprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH2), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic a-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly a-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranespt_BR
dc.description.sponsorship(JSPS) Japan Society for the Promotion of Sciencept_BR
dc.description.sponsorship(MEXT-JA) Ministério da Educação, Cultura, Desporto, Ciência e Tecnologia do Japãopt_BR
dc.format.extent155pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofToxinspt_BR
dc.rightsOpen accesspt_BR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_BR
dc.titleNew mastoparan peptides in the venom of the solitary eumenine wasp eumenes micadopt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.3390/toxins11030155pt_BR
dc.identifier.urlhttp://dx.doi.org/10.3390/toxins11030155pt_BR
dc.contributor.externalUniversity of Toyamapt_BR
dc.contributor.external(UFOPA) Universidade Federal do Oeste do Parápt_BR
dc.contributor.external(UESC) Universidade Estadual de Santa Cruzpt_BR
dc.contributor.external(NIBIO) National Institute of Biomedical Innovationpt_BR
dc.contributor.externalHiroshima Universitypt_BR
dc.contributor.externalKitasato Universitypt_BR
dc.identifier.citationvolume11pt_BR
dc.identifier.citationissue3pt_BR
dc.subject.keywordsolitary wasppt_BR
dc.subject.keywordvenompt_BR
dc.subject.keywordmastoparan peptidept_BR
dc.subject.keywordlinear cationic a-helical peptidept_BR
dc.subject.keywordamphipathic a-helix structurept_BR
dc.relation.ispartofabbreviatedToxinspt_BR
dc.identifier.citationabntv. 11, n. 3, 155, mar. 2019pt_BR
dc.identifier.citationvancouver2019 Mar;11(3):155pt_BR
dc.contributor.butantanRangel, Marisa|:Pesquisador|:Lab. Imunopatologia|:pt_BR
dc.sponsorship.butantan(JSPS) Japan Society for the Promotion of Science¦¦15K07805pt_BR
dc.sponsorship.butantan(MEXT-JA) Ministério da Educação, Cultura, Desporto, Ciência e Tecnologia do Japão¦¦pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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