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dc.contributor.authorCirilo Gimenes, Sarah Natalie-
dc.contributor.authorFerreira, Francis Barbosa-
dc.contributor.authorPortella Silveira, Ana Carolina-
dc.contributor.authorRodrigues, Renata Santos-
dc.contributor.authorGeraldo Yoneyama, Kelly Aparecida-
dc.contributor.authorSantos, Juliana Izabel dos-
dc.contributor.authorMattos Fontes, Marcos Roberto de-
dc.contributor.authorCampos Brites, Vera Lucia de-
dc.contributor.authorQuagliatto Santos, Andre Luiz-
dc.contributor.authorBorges, Marcia Helena-
dc.contributor.authorLopes, Daiana Silva-
dc.contributor.authorRodrigues, Veridiana M.-
dc.identifier.citationToxicon. Oxford: Pergamon-elsevier Science Ltd, v. 81, p. 58-66, 2014.-
dc.description.abstractIn the present work, we describe the isolation and partial structural and biochemical characterization of the first phospholipase A(2) inhibitor (gamma PLI) from Crotalus durissus collilineatus (Cdc) snake serum. Initially, the Cdc serum was subjected to a Q-Sepharose ion exchange column, producing six peaks at 280 nm absorbance (Q1-Q6). Subsequently, Q4 fraction was submitted to affinity chromatography with immobilized PLA(2) BnSP-7, a step that resulted in two fractions (NHS-1 and NHS-2). The latter contained the inhibitor, denominated gamma CdcPLI. The molecular mass of gamma CdcPLI, determined by Matrix-Assisted Laser Desorption Ionization Time-of-Flight (MALDI-TOF), was 22,340 Da. Partial sequences obtained by Edman degradation and by mass spectrometry (MALDI-TOF/TOF), showed similarity, as expected, to other related inhibitors. Circular dichroism (CD) analysis showed the presence of approximately 22% alpha helices and 29% beta sheets in the protein secondary structure. Additionally, CD studies also indicated no significant changes in the secondary structure of gamma CdcPLI when it is complexed to BpPLA(2)-TXI. On the other hand, dynamic light scattering (DLS) assays showed a temperature-dependent oligomerization behavior for this inhibitor. Biochemical analyses showed gamma CdcPLI was able to inhibit the enzymatic, cytotoxic and myotoxic activities of PLA(2)s. Structural and functional studies performed on this inhibitor may elucidate the action mechanisms of PLA(2) inhibitors. In addition, we hope this study may contribute to investigating the potential use of these inhibitors for the treatment of snakebite or inflammatory diseases in which PLA(2)s may be involved. (C) 2014 Elsevier Ltd. All rights reserved.en
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)-
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipInstituto Nacional de Ciencia em Tecnologia de Toxinas-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.description.sponsorshipUniversidade Federal de Uberlandia-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectCrotalus durissus collilineatusen
dc.subjectPhospholipase A(2) inhibitorsen
dc.subjectInhibitor gamma-typeen
dc.subjectPhospholipase A(2)en
dc.titleIsolation and biochemical characterization of a gamma-type phospholipase A2 inhibitor from Crotalus durissus collilineatus snake serumen
dc.contributor.institutionUniversidade Federal de Uberlândia (UFU)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionInst Nacl Ciencia & Tecnol Nanobiofarmaceut-
dc.description.affiliationUniv Fed Uberlandia, Inst Genet & Bioquim, BR-38400902 Uberlandia, MG, Brazil-
dc.description.affiliationUniv Estadual Paulista, UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil-
dc.description.affiliationFUNED, Fundacao Ezequiel Dias, Belo Horizonte, MG, Brazil-
dc.description.affiliationInst Nacl Ciencia & Tecnol Nanobiofarmaceut, INCT, Belo Horizonte, MG, Brazil-
dc.description.affiliationUniv Fed Uberlandia, Inst Biol, BR-38400902 Uberlandia, MG, Brazil-
dc.description.affiliationUniv Fed Uberlandia, Fac Med Vet, BR-38400902 Uberlandia, MG, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP, Brazil-
dc.rights.accessRightsAcesso restrito-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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