Oxidation of amino acids by chlorpromazine cation radical and co-catalysis by chlorpromazine

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorXimenes, Valdecir Farias [UNESP]
dc.creatorQuaggio, Giovana Brino [UNESP]
dc.creatorGraciane, Fernanda Silva [UNESP]
dc.creatorMenezes, Manoel Lima de [UNESP]
dc.date2016-01-28T16:56:51Z
dc.date2016-01-28T16:56:51Z
dc.date2012
dc.date.accessioned2023-09-12T08:17:48Z
dc.date.available2023-09-12T08:17:48Z
dc.identifierhttp://dx.doi.org/10.4236/pp.2012.31005
dc.identifierPharmacology and Pharmacy, v. 3, n. 1, p. 29-36, 2012.
dc.identifier2157-9423
dc.identifierhttp://hdl.handle.net/11449/133848
dc.identifier10.4236/pp.2012.31005
dc.identifier4066413997908572
dc.identifier4659698040759224
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8783099
dc.descriptionThe 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.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionUniversidade 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.descriptionUniversidade 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.format29-36
dc.languageeng
dc.publisherSciRes
dc.relationPharmacology and Pharmacy
dc.rightsAcesso restrito
dc.sourceCurrículo Lattes
dc.subjectTryptophan
dc.subjectTyrosine
dc.subjectNitrite
dc.subjectChlorpromazine
dc.subjectHorseradish peroxidase
dc.titleOxidation of amino acids by chlorpromazine cation radical and co-catalysis by chlorpromazine
dc.typeArtigo


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