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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/133848
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dc.contributor.authorXimenes, Valdecir Farias-
dc.contributor.authorQuaggio, Giovana Brino-
dc.contributor.authorGraciane, Fernanda Silva-
dc.contributor.authorMenezes, Manoel Lima de-
dc.date.accessioned2016-01-28T16:56:51Z-
dc.date.accessioned2016-10-25T21:29:02Z-
dc.date.available2016-01-28T16:56:51Z-
dc.date.available2016-10-25T21:29:02Z-
dc.date.issued2012-
dc.identifierhttp://dx.doi.org/10.4236/pp.2012.31005-
dc.identifier.citationPharmacology and Pharmacy, v. 3, n. 1, p. 29-36, 2012.-
dc.identifier.issn2157-9423-
dc.identifier.urihttp://hdl.handle.net/11449/133848-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/133848-
dc.description.abstractThe long-tem use of chlorpromazine (CPZ) may cause severe side effects. This property of CPZ might be related to pro-oxidant effects of the chlorpromazine cation radical (CPZ•+), which can be easily generated by catalytic action of peroxidases, including the neutrophil myeloperoxidase (MPO) and by methemoglobin. Aiming the comprehension of a putative physiological effect of CPZ•+ upon biomolecules, in this work we studied the reactivity of CPZ•+ with amino acids and the co-catalytic effect of CPZ during the oxidation of amino acids by horseradish peroxidase (HRP)/H2O2 system. We also studied whether natural blood plasma components as ascorbic acid, uric acid and nitrite could inhibit the oxidative effect of CPZ•+. We found that tryptophan, tyrosine and cysteine were easily oxidized by pure CPZ•+. Other amino acids as methionine, glycine, phenylalanine, aspartic acid and lysine were unreactive. The decomposition of CPZ•+ was exacerbated by uric acid, ascorbic acid and nitrite, provoking inhibition in the amino acids oxidation. In experiments with HRP/H2O2, and using CPZ as a co-catalyst, a strong effect upon oxidation of tryptophan, tyrosine and cysteine was obtained. It was also found that tryptophan was more reactive than tyrosine with CPZ•+, a feature that could be related to the recently described favorable interaction between tryptophan and CPZ. The use of CPZ as a co-catalyst is discussed regarding its role in the efficient oxidation of tryptophan.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
dc.format.extent29-36-
dc.language.isoeng-
dc.publisherSciRes-
dc.sourceCurrículo Lattes-
dc.subjectTryptophanen
dc.subjectTyrosineen
dc.subjectNitriteen
dc.subjectChlorpromazineen
dc.subjectHorseradish peroxidaseen
dc.titleOxidation of amino acids by chlorpromazine cation radical and co-catalysis by chlorpromazineen
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Faculdade de Ciências (FC), Departamento de Química, Av. Eng. Luiz Edmundo Carrijo Coube, s/n, Vargem Limpa, CEP 17033360, Bauru, SP, Brasil-
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho (UNESP), Faculdade de Ciências (FC), Departamento de Química, Av. Eng. Luiz Edmundo Carrijo Coube, s/n, Vargem Limpa, CEP 17033360, Bauru, SP, Brasil-
dc.identifier.doi10.4236/pp.2012.31005-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofPharmacology and Pharmacy-
dc.identifier.lattes4066413997908572-
dc.identifier.lattes4659698040759224-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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