Analogs of the scorpion venom peptide stigmurin: structural assessment, toxicity, and increased antimicrobial activity

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dc.contributorLaboratório de Bacteriologiapt_BR
dc.contributor.authorParente, Adriana M. S.pt_BR
dc.contributor.authorDaniele-Silva, Alessandrapt_BR
dc.contributor.authorFurtado, Allanny A.pt_BR
dc.contributor.authorMelo, Menilla A.pt_BR
dc.contributor.authorLacerda, Ariane F.pt_BR
dc.contributor.authorQueiroz, Moacirpt_BR
dc.contributor.authorMoreno, Cláudiapt_BR
dc.contributor.authorSantos, Elizabethpt_BR
dc.contributor.authorRocha, Hugo A. O.pt_BR
dc.contributor.authorBarbosa, Euzébio G.pt_BR
dc.contributor.authorCarvalho, Eneaspt_BR
dc.contributor.authorSilva-Junior, Arnóbio A.pt_BR
dc.contributor.authorSilva, Marcelo S.pt_BR
dc.contributor.authorFernandes-Pedrosa, Matheus de F.pt_BR
dc.identifier.citationParente AM.S., Daniele-Silva A, Furtado AA., Melo MA., Lacerda AF., Queiroz M, et al. Analogs of the scorpion venom peptide stigmurin: structural assessment, toxicity, and increased antimicrobial activity. Toxins. 2018 Apr;10(4):161. doi:10.3390/toxins10040161.pt_BR
dc.description.abstractScorpion venom is a rich source of biologically active components and various peptides with high-potential therapeutic use that have been characterized for their antimicrobial and antiproliferative activities. Stigmurin is a peptide identified from the Tityus stigmurus venom gland with high antibacterial and antiproliferative activities and low toxicity. Amino acid substitutions in peptides without a disulfide bridge sequence have been made with the aim of reducing their toxicity and increasing their biological activities. The purpose of this study was to evaluate the structural conformation and structural stability, as well as antimicrobial, antiproliferative, and hemolytic activities of two peptide analogs to Stigmurin, denominated StigA6 and StigA16. In silico analysis revealed the -helix structure for both analog peptides, which was confirmed by circular dichroism. Data showed that the net charge and hydrophobic moment of the analog peptides were higher than those for Stigmurin, which can explain the increase in antimicrobial activity presented by them. Both analog peptides exhibited activity on cancerous cells similar to the native peptide; however, they were less toxic when tested on the normal cell line. These results reveal a potential biotechnological application of the analog peptides StigA6 and StigA16 as prototypes to new therapeutic agents.pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Apoio à Pesquisa do Rio Grande do Norte (FAPERN)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.description.sponsorshipGlobal Health and Tropical Medicine (GHTM)pt_BR
dc.description.sponsorshipEuropean Commission (EC)pt_BR
dc.rightsOpen Accesspt_BR
dc.titleAnalogs of the scorpion venom peptide stigmurinpt_BR
dc.contributor.externalUniversidade Federal do Rio Grande do Norte (UFRN)¦¦Brasilpt_BR
dc.contributor.externalUniversidade Nova de Lisboa (NOVA)¦¦Portugalpt_BR
dc.title.substructural assessment, toxicity, and increased antimicrobial activitypt_BR
dc.subject.keywordantimicrobial peptidept_BR
dc.subject.keywordscorpion venompt_BR
dc.subject.keywordstructure-activity relationshippt_BR
dc.subject.keywordanalog peptidespt_BR
dc.identifier.citationabntv. 10, n. 4, 161, abr. 2018pt_BR
dc.identifier.citationvancouver2018 Apr;10(4):161pt_BR
dc.contributor.butantanCarvalho, Eneas|:Pesquisador|:Laboratório de Bacteriologia|:pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦pt_BR
dc.sponsorship.butantanEuropean Commission (EC)¦¦305937pt_BR
dc.sponsorship.butantanFundação de Apoio à Pesquisa do Rio Grande do Norte (FAPERN)¦¦PRONEM/2011pt_BR
dc.sponsorship.butantanGlobal Health and Tropical Medicine (GHTM)¦¦GHTM-UID/multi/04413/2013pt_BR
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