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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleModulation of the Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus cascavella Induced by Naringinpt_BR
dc.contributor.authorSantos, MLpt_BR
dc.contributor.authorToyama, DOpt_BR
dc.contributor.authorOliveira, SCBpt_BR
dc.contributor.authorCotrim, CApt_BR
dc.contributor.authorDiz, EBSpt_BR
dc.contributor.authorFagundes, FHRpt_BR
dc.contributor.authorSoares, VCGpt_BR
dc.contributor.authorAparicio, Rpt_BR
dc.contributor.authorToyama, MHpt_BR
unicamp.authorToyama, Marcos H. UNESP CLP, Lab Macromol Quim, Sao Paulo, Brazilpt_BR
unicamp.authorSantos, Marcelo L. Aparicio, Ricardo Univ Estadual Campinas, Inst Quim, Lab Biol Estrutural & Cristalog, Sao Paulo, Brazilpt_BR
unicamp.authorToyama, Daniela O. Univ Presbiteriana Mackenzie, CCBS, Sao Paulo, Brazilpt_BR
unicamp.authorOliveira, Simone C. B. Cotrim, Camila A. Diz-Filho, Eduardo B. S. Fagundes, Fabio H. R. Soares, Veronica C. G. Univ Estadual Campinas, Inst Biol, Dept Bioquim, Sao Paulo, Brazilpt_BR
dc.subjectsecretoy phospholipase A2pt_BR
dc.subjectCrotalus durissus cascavellapt_BR
dc.subjectenzymatic activity pharmacological effectspt_BR
dc.subjectsmall angle X-ray scatteringpt_BR
dc.subject.wosProtein-structure Predictionpt_BR
dc.subject.wosSmall-angle Scatteringpt_BR
dc.subject.wosAntiinflammatory Activitypt_BR
dc.subject.wosCollilineatus Venompt_BR
dc.subject.wosPlant Flavonoidspt_BR
dc.subject.wosTerrificus Venompt_BR
dc.subject.wosA(2) Inhibitorspt_BR
dc.description.abstractIn this work we have characterized the action of the naringin, a flavonoid found in grapefruit and known for its various pharmacological effects, which include antioxidant, blood lipid lowering and anticancer activity, on the structure and biochemical activities of a secretory phospholipase A (sPLA2) from Crotalus durissus cascavella, an important protein involved in the releasinge of arachidonic acid in phospholipid membranes. sPLA2 was incubated with naringin (mol:mol) at 37 degrees C and a discrete reduction in the UV scanning signal and a modification of the circular dichroism spectra were observed after treatment with naringin, suggesting modifications of the secondary structure of the protein. This flavonoid was able to decrease enzymatic activity and some pharmacological effects, such as myonecrosis, platelet aggregation, and neurotoxic activity caused by sPLA2, however, the inflammatory effect was not affected by naringin. In addition, small angle X-ray scattering (SAXS) data were collected for sPLA2 and naringin-treated sPLA2 to evaluate possible modifications of the protein structure. These structural investigations have shown that sPLA2 is an elongated dimer in solution and after treatment with naringin a conformational change in the dimeric configuration was observed. Our results suggest that structural modification may be correlated with the loss of enzymatic activity and alterations in pharmacological
dc.publisherMdpi Agpt_BR
dc.identifier.citationMolecules. Mdpi Ag, v. 16, n. 1, n. 738, n. 761, 2011.pt_BR
dc.sourceWeb of Sciencept_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorship1Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorship1Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.provenanceMade available in DSpace on 2014-07-30T14:03:33Z (GMT). No. of bitstreams: 0 Previous issue date: 2011en
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