Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes

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dc.contributorLETA - Laboratório de Toxinologia Aplicadapt_BR
dc.contributor.authorAguirre, Elisa Chaparropt_BR
dc.contributor.authorSegura Ramirez, Paula Jimenapt_BR
dc.contributor.authorAlves, Flávio L.pt_BR
dc.contributor.authorRiske, Karin A.pt_BR
dc.contributor.authorMiranda, Antoniopt_BR
dc.contributor.authorSilva Junior, Pedro Ismael dapt_BR
dc.date.accessioned2020-07-09T21:25:21Z-
dc.date.available2020-07-09T21:25:21Z-
dc.date.issued2019pt_BR
dc.identifier.citationAguirre EC, Segura-Ramirez PJ, Alves FL., Riske KA., Miranda A, Silva Junior PI. Antimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipes. Sci. rep.. 2019 Sep;9:13631. doi:10.1038/s41598-019-50061-y.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2851-
dc.description.abstractOne of the most important cellular events in arthropods is the moulting of the cuticle (ecdysis). This process allows them to grow until they reach sexual maturity. Nevertheless, during this stage, the animals are highly exposed to pathogens. Consequently, it can be assumed that arthropods counter with an efficient anti-infective strategy that facilitates their survival during ecdysis. Herein, we characterized a novel antimicrobial peptide called Pinipesin, present in the exuviae extract of the centipede Scolopendra subspinipes subspinipes. The antimicrobial activity of Pinipesin was tested. The haemolytic activity of the peptide was evaluated and its possible mechanism of action was investigated. Identification was carried out by mass spectrometry analysis. Pinipesin displayed potent antimicrobial effects against different microorganisms and showed low haemolytic effects against human erythrocytes at high concentrations. It has a monoisotopic mass of 1213.57 Da, its sequence exhibited high similarity with some cuticular proteins, and it might act intracellularly by interfering with protein synthesis. Our data suggest that Pinipesin might be part of a prophylactic immune response during the ecdysis process of centipedes. Therefore, it is a promising candidate for the development of non-conventional antibiotics that could help fight infectious diseases and represents an exciting discovery for this taxon.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.format.extent13631pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofScientific Reportspt_BR
dc.rightsOpen Accesspt_BR
dc.titleAntimicrobial activity and mechanism of action of a novel peptide present in the ecdysis process of centipede Scolopendra subspinipes subspinipespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1038/s41598-019-50061-ypt_BR
dc.identifier.urlhttps://doi.org/10.1038/s41598-019-50061-ypt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.identifier.citationvolume9pt_BR
dc.relation.ispartofabbreviatedSci reppt_BR
dc.identifier.citationabntv. 9, 13631, sep. 2019pt_BR
dc.identifier.citationvancouver2019 Sep;9:13631pt_BR
dc.contributor.butantanSegura Ramirez, Paula Jimena|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:Autor de correspondênciapt_BR
dc.contributor.butantanSilva Junior, Pedro Ismael da|:Pesquisador|:Laboratório Especial de Toxinologia Aplicada (LETA)|:pt_BR
dc.contributor.butantanAguirre, Elisa Chaparro|:Aluno|:Laboratório Especial de Toxinologia Aplicada (LETA)|:PrimeiroAutorpt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦472744/2012-7pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2013/07467-1pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.openairetypeArticle-
item.fulltextCom Texto completo-
item.grantfulltextopen-
item.languageiso639-1English-
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