Sarconesin II, a new antimicrobial peptide isolated from Sarconesiopsis magellanica excretions and secretions

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dc.contributorLaboratório de Toxinologia Aplicadapt_BR
dc.contributorLab. Bacteriologiapt_BR
dc.contributorLCC - Laboratório de Ciclo Celularpt_BR
dc.contributor.authorDíaz-Roa, Andreapt_BR
dc.contributor.authorEspinoza-Culupú, Abrahampt_BR
dc.contributor.authorTorres-García, Orlandopt_BR
dc.contributor.authorBorges, Monamaris Marquespt_BR
dc.contributor.authorAvino, Ivan Novaskipt_BR
dc.contributor.authorAlves, Flávio L.pt_BR
dc.contributor.authorMiranda, Antoniopt_BR
dc.contributor.authorPatarroyo, Manuel A.pt_BR
dc.contributor.authorSilva Junior, Pedro Ismael dapt_BR
dc.contributor.authorBello, Felio J.pt_BR
dc.date.accessioned2020-07-09T21:24:16Z-
dc.date.available2020-07-09T21:24:16Z-
dc.date.issued2019pt_BR
dc.identifier.citationDíaz-Roa A, Espinoza-Culupú AO, Torres-García O, Borges MM, Avino IN, Alves FL., et al. Sarconesin II, a new antimicrobial peptide isolated from Sarconesiopsis magellanica excretions and secretions. Molecules. 2019 May;24:2077. doi:10.3390/molecules24112077.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2770-
dc.description.abstractAntibiotic resistance is at dangerous levels and increasing worldwide. The search for new antimicrobial drugs to counteract this problem is a priority for health institutions and organizations, both globally and in individual countries. Sarconesiopsis magellanica blowfly larval excretions and secretions (ES) are an important source for isolating antimicrobial peptides (AMPs). This study aims to identify and characterize a new S. magellanica AMP. RP-HPLC was used to fractionate ES, using C18 columns, and their antimicrobial activity was evaluated. The peptide sequence of the fraction collected at 43.7 min was determined by mass spectrometry (MS). Fluorescence and electronic microscopy were used to evaluate the mechanism of action. Toxicity was tested on HeLa cells and human erythrocytes; physicochemical properties were evaluated. The molecule in the ES was characterized as sarconesin II and it showed activity against Gram-negative (Escherichia coli MG1655, Pseudomonas aeruginosa ATCC 27853, P. aeruginosa PA14) and Gram-positive (Staphylococcus aureus ATCC 29213, Micrococcus luteus A270) bacteria. The lowest minimum inhibitory concentration obtained was 1.9 µM for M. luteus A270; the AMP had no toxicity in any cells tested here and its action in bacterial membrane and DNA was confirmed. Sarconesin II was documented as a conserved domain of the ATP synthase protein belonging to the Fli-1 superfamily. The data reported here indicated that peptides could be alternative therapeutic candidates for use in infections against Gram-negative and Gram-positive bacteria and eventually as a new resource of compounds for combating multidrug-resistant bacteria.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.sponsorshipCOLCIENCIAS-UANpt_BR
dc.format.extent2077pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofMoleculespt_BR
dc.rightsOpen accesspt_BR
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/pt_BR
dc.titleSarconesin II, a new antimicrobial peptide isolated from Sarconesiopsis magellanica excretions and secretionspt_BR
dc.typeArticlept_BR
dc.rights.licenseCC BYpt_BR
dc.identifier.doi10.3390/molecules24112077pt_BR
dc.identifier.urlhttps://doi.org/10.3390/molecules24112077pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.contributor.externalUniversidad del Rosario¦¦Colômbiapt_BR
dc.contributor.externalUniversidad Antonio Nariño¦¦Colômbiapt_BR
dc.contributor.externalUniversidade Federal de São Paulo (UNIFESP)¦¦Brasilpt_BR
dc.contributor.externalFundación Instituto de Inmunología de Colombia (FIDIC)¦¦Colômbiapt_BR
dc.contributor.externalUniversidad de La Salle¦¦Colômbiapt_BR
dc.identifier.citationvolume24pt_BR
dc.subject.keywordantimicrobial peptidept_BR
dc.subject.keywordSarconesiopsis magellanicapt_BR
dc.subject.keywordCalliphoridaept_BR
dc.subject.keyworddrugpt_BR
dc.subject.keywordalpha-helixpt_BR
dc.relation.ispartofabbreviatedMoleculespt_BR
dc.identifier.citationabntv. 24, 2077, maio 2019pt_BR
dc.identifier.citationvancouver2019 May;24:2077pt_BR
dc.contributor.butantanDíaz-Roa, Andrea|:Aluno|:Laboratório de Toxinologia Aplicada|:PrimeiroAutorpt_BR
dc.contributor.butantanEspinoza-Culupú, Abraham|:Aluno|:Lab. Bacteriologia|:pt_BR
dc.contributor.butantanBorges, Monamaris Marques|:Pesquisador|:Lab. Bacteriologia|:pt_BR
dc.contributor.butantanAvino, Ivan Novaski|:Técnico|:LCC - Laboratório de Ciclo Celular|:pt_BR
dc.contributor.butantanSilva Junior, Pedro Ismael da|:Pesquisador|:Laboratório de Toxinologia Aplicada|:pt_BR
dc.sponsorship.butantanCOLCIENCIAS-UAN¦¦FP44842-384-2016pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦472744/2012-7pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦13/07467-1pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.languageiso639-1English-
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