Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens

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dc.contributorLaboratório de Toxinologia Aplicadapt_BR
dc.contributor.authorPedron, Cibele Nicolaskipt_BR
dc.contributor.authorAraujo, Irispt_BR
dc.contributor.authorSilva Junior, Pedro Ismael dapt_BR
dc.contributor.authorSilva, Fernanda Dias dapt_BR
dc.contributor.authorTorres, Marcelo Der Torossianpt_BR
dc.contributor.authorOliveira Junior, Vani Xavierpt_BR
dc.date.accessioned2020-07-09T21:24:18Z-
dc.date.available2020-07-09T21:24:18Z-
dc.date.issued2019pt_BR
dc.identifier.citationPedron CN, Araujo I, Silva Junior PI, Silva FD, Torres MDT, Oliveira Junior VX. Repurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogens. Bioorg. chem.. 2019 Sept;90:103038. doi:10.1016/j.bioorg.2019.103038.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2772-
dc.description.abstractVmCT1 is a cationic antimicrobial peptide (AMP) from the venom of the scorpion Vaejovis mexicanus. VmCT1 and analogs were designed with single substitutions for verifying the influence of changes in physicochemical features described as important for AMPs antimicrobial and hemolytic activities, as well as their effect on VmCT1 analogs resistance against proteases action. The increase of the net positive charge by the introduction of an arginine residue in positions of the hydrophilic face of the helical structure affected directly the antimicrobial activity. Arg-substituted analogs presented activity against Gram-negative bacteria from the ESKAPE list of pathogens that were not observed for VmCT1. Additionally, peptides with higher net positive charge presented increased antimicrobial activity with values ranging from 0.39 to 12.5 µmol L-1 against Gram-positive and Gram-negative bacteria and fungi. The phenylalanine substitution by glycine (position 1), and the valine substitution by a proline residue (position 8) led to analogs with lower hemolytic activity (at concentrations 50 and 100 µmol L-1, respectively). These results revealed that it is possible to modulate the biological activities of VmCT1 derivatives by designing single substituted-analogs as prospective therapeutics against bacteria and fungi.pt_BR
dc.description.sponsorship(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.format.extent103038pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofBioorganic Chemistrypt_BR
dc.titleRepurposing the scorpion venom peptide VmCT1 into an active peptide against Gram-negative ESKAPE pathogenspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.bioorg.2019.103038pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.bioorg.2019.103038pt_BR
dc.contributor.external(UFABC) Universidade Federal do ABCpt_BR
dc.contributor.external(UNIFESP) Universidade Federal de São Paulopt_BR
dc.contributor.externalUniversity of Pennsylvaniapt_BR
dc.identifier.citationvolume90pt_BR
dc.subject.keywordantimicrobial peptidept_BR
dc.subject.keywordVmCT1pt_BR
dc.subject.keywordstructure-activity relationshippt_BR
dc.subject.keywordScorpion venom peptidept_BR
dc.relation.ispartofabbreviatedBioorg chempt_BR
dc.identifier.citationabntv. 90, 103038, set. 2019pt_BR
dc.identifier.citationvancouver2019 Sept;90:103038pt_BR
dc.contributor.butantanSilva Junior, Pedro Ismael da|:Pesquisador|:Laboratório de Toxinologia Aplicada|:pt_BR
dc.sponsorship.butantan(CAPES) Coordenação de Aperfeiçoamento de Pessoal de Nível Superior¦¦pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2017/03046-2pt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2014/04507-5pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.grantfulltextembargo_29990101-
item.languageiso639-1English-
item.fulltextCom Texto completo-
item.openairetypeArticle-
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