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DC Field | Value | Language |
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dc.contributor.author | Ximenes, Valdecir Farias | - |
dc.contributor.author | Quaggio, Giovana Brino | - |
dc.contributor.author | Graciane, Fernanda Silva | - |
dc.contributor.author | Menezes, Manoel Lima de | - |
dc.date.accessioned | 2016-01-28T16:56:51Z | - |
dc.date.accessioned | 2016-10-25T21:29:02Z | - |
dc.date.available | 2016-01-28T16:56:51Z | - |
dc.date.available | 2016-10-25T21:29:02Z | - |
dc.date.issued | 2012 | - |
dc.identifier | http://dx.doi.org/10.4236/pp.2012.31005 | - |
dc.identifier.citation | Pharmacology and Pharmacy, v. 3, n. 1, p. 29-36, 2012. | - |
dc.identifier.issn | 2157-9423 | - |
dc.identifier.uri | http://hdl.handle.net/11449/133848 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/133848 | - |
dc.description.abstract | The 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.sponsorship | Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) | - |
dc.description.sponsorship | Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) | - |
dc.format.extent | 29-36 | - |
dc.language.iso | eng | - |
dc.publisher | SciRes | - |
dc.source | Currículo Lattes | - |
dc.subject | Tryptophan | en |
dc.subject | Tyrosine | en |
dc.subject | Nitrite | en |
dc.subject | Chlorpromazine | en |
dc.subject | Horseradish peroxidase | en |
dc.title | Oxidation of amino acids by chlorpromazine cation radical and co-catalysis by chlorpromazine | en |
dc.type | outro | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.description.affiliation | Universidade 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.affiliationUnesp | Universidade 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.doi | 10.4236/pp.2012.31005 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | Pharmacology and Pharmacy | - |
dc.identifier.lattes | 4066413997908572 | - |
dc.identifier.lattes | 4659698040759224 | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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