A simple electrochemical method to monitor an azo dye reaction with a liver protein
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.ab.2018.05.016 http://hdl.handle.net/11449/179905 |
Resumo: | Disperse Orange 37 (DO37) is an efficient azo dye for dyeing synthetic textile materials owing to its resistance to degradation that may also be harmful to humans as DO37 is not entirely eliminated in wastewater treatment. In this paper, we demonstrate that DO37 is bleached by reduced glutathione (GSH) in a reaction catalyzed by glutathione-s-transferase (GST), a phase II detoxification enzyme. The reaction included a nucleophilic attack involving sulfhydryl groups, confirmed using density functional theory (DFT) calculations. DO37 also induced quenching in the fluorescence of GST through static suppression. The reaction was determined using differential pulse voltammetry (DPV) by monitoring the oxidation peak at 0.65 V of GSH sulfhydryl group. Quantitative estimation of the product reaction could be made by measuring an additional oxidation peak at 0.91 V which increased linearly with DO37 concentration. These electrochemical determinations were made possible by preconcentrating the reaction product on a graphite-epoxy electrode with immobilization of GST onto magnetite nanoparticles. Straightforward biological implications from the results are associated with the known toxicity of azo dyes such as DO37, which has been proven here to interact strongly with both GSH and the liver enzyme GST, and may induce hepatocarcinogenesis or other types of cancer. |
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A simple electrochemical method to monitor an azo dye reaction with a liver proteinDisperse Orange 37 (DO37) is an efficient azo dye for dyeing synthetic textile materials owing to its resistance to degradation that may also be harmful to humans as DO37 is not entirely eliminated in wastewater treatment. In this paper, we demonstrate that DO37 is bleached by reduced glutathione (GSH) in a reaction catalyzed by glutathione-s-transferase (GST), a phase II detoxification enzyme. The reaction included a nucleophilic attack involving sulfhydryl groups, confirmed using density functional theory (DFT) calculations. DO37 also induced quenching in the fluorescence of GST through static suppression. The reaction was determined using differential pulse voltammetry (DPV) by monitoring the oxidation peak at 0.65 V of GSH sulfhydryl group. Quantitative estimation of the product reaction could be made by measuring an additional oxidation peak at 0.91 V which increased linearly with DO37 concentration. These electrochemical determinations were made possible by preconcentrating the reaction product on a graphite-epoxy electrode with immobilization of GST onto magnetite nanoparticles. Straightforward biological implications from the results are associated with the known toxicity of azo dyes such as DO37, which has been proven here to interact strongly with both GSH and the liver enzyme GST, and may induce hepatocarcinogenesis or other types of cancer.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Institute of Chemistry São Paulo State University (UNESP)São Carlos Institute of Physics University of São Paulo, P.O Box 369Institute of Chemistry Autonomous University of Barcelona (UAB)Institute of Chemistry São Paulo State University (UNESP)FAPESP: 2012/15543-7FAPESP: 2013/14262-7FAPESP: 2016/00991-5Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Autonomous University of Barcelona (UAB)Materón, Elsa Maria [UNESP]Marchetto, Reinaldo [UNESP]Araujo, Angela Regina [UNESP]Vega-Chacon, Jaime [UNESP]Pividori, Maria I.Jafelicci, Miguel [UNESP]Shimizu, Flavio M.Oliveira, Osvaldo N.Zanoni, Maria Valnice Boldrin [UNESP]2018-12-11T17:37:13Z2018-12-11T17:37:13Z2018-07-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article46-53application/pdfhttp://dx.doi.org/10.1016/j.ab.2018.05.016Analytical Biochemistry, v. 553, p. 46-53.1096-03090003-2697http://hdl.handle.net/11449/17990510.1016/j.ab.2018.05.0162-s2.0-850476492072-s2.0-85047649207.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAnalytical Biochemistry0,6330,633info:eu-repo/semantics/openAccess2023-12-01T06:16:42Zoai:repositorio.unesp.br:11449/179905Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-01T06:16:42Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
title |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
spellingShingle |
A simple electrochemical method to monitor an azo dye reaction with a liver protein Materón, Elsa Maria [UNESP] |
title_short |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
title_full |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
title_fullStr |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
title_full_unstemmed |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
title_sort |
A simple electrochemical method to monitor an azo dye reaction with a liver protein |
author |
Materón, Elsa Maria [UNESP] |
author_facet |
Materón, Elsa Maria [UNESP] Marchetto, Reinaldo [UNESP] Araujo, Angela Regina [UNESP] Vega-Chacon, Jaime [UNESP] Pividori, Maria I. Jafelicci, Miguel [UNESP] Shimizu, Flavio M. Oliveira, Osvaldo N. Zanoni, Maria Valnice Boldrin [UNESP] |
author_role |
author |
author2 |
Marchetto, Reinaldo [UNESP] Araujo, Angela Regina [UNESP] Vega-Chacon, Jaime [UNESP] Pividori, Maria I. Jafelicci, Miguel [UNESP] Shimizu, Flavio M. Oliveira, Osvaldo N. Zanoni, Maria Valnice Boldrin [UNESP] |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) Autonomous University of Barcelona (UAB) |
dc.contributor.author.fl_str_mv |
Materón, Elsa Maria [UNESP] Marchetto, Reinaldo [UNESP] Araujo, Angela Regina [UNESP] Vega-Chacon, Jaime [UNESP] Pividori, Maria I. Jafelicci, Miguel [UNESP] Shimizu, Flavio M. Oliveira, Osvaldo N. Zanoni, Maria Valnice Boldrin [UNESP] |
description |
Disperse Orange 37 (DO37) is an efficient azo dye for dyeing synthetic textile materials owing to its resistance to degradation that may also be harmful to humans as DO37 is not entirely eliminated in wastewater treatment. In this paper, we demonstrate that DO37 is bleached by reduced glutathione (GSH) in a reaction catalyzed by glutathione-s-transferase (GST), a phase II detoxification enzyme. The reaction included a nucleophilic attack involving sulfhydryl groups, confirmed using density functional theory (DFT) calculations. DO37 also induced quenching in the fluorescence of GST through static suppression. The reaction was determined using differential pulse voltammetry (DPV) by monitoring the oxidation peak at 0.65 V of GSH sulfhydryl group. Quantitative estimation of the product reaction could be made by measuring an additional oxidation peak at 0.91 V which increased linearly with DO37 concentration. These electrochemical determinations were made possible by preconcentrating the reaction product on a graphite-epoxy electrode with immobilization of GST onto magnetite nanoparticles. Straightforward biological implications from the results are associated with the known toxicity of azo dyes such as DO37, which has been proven here to interact strongly with both GSH and the liver enzyme GST, and may induce hepatocarcinogenesis or other types of cancer. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12-11T17:37:13Z 2018-12-11T17:37:13Z 2018-07-15 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.ab.2018.05.016 Analytical Biochemistry, v. 553, p. 46-53. 1096-0309 0003-2697 http://hdl.handle.net/11449/179905 10.1016/j.ab.2018.05.016 2-s2.0-85047649207 2-s2.0-85047649207.pdf |
url |
http://dx.doi.org/10.1016/j.ab.2018.05.016 http://hdl.handle.net/11449/179905 |
identifier_str_mv |
Analytical Biochemistry, v. 553, p. 46-53. 1096-0309 0003-2697 10.1016/j.ab.2018.05.016 2-s2.0-85047649207 2-s2.0-85047649207.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Analytical Biochemistry 0,633 0,633 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
46-53 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1799965134738685952 |