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Data on the catalytic mechanism of thiol peroxidase mimics

We have recently reported SAR data describing the pharmacological activity of a series of phenyl alkyl selenides and tellurides which catalyse the oxidation of thiols by hydrogen peroxide (H(2)O(2)), “The design of redox active thiol peroxidase mimics: dihydrolipoic acid recognition correlates with...

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Detalles Bibliográficos
Autores principales: Zadehvakili, B., Giles, N.M., Fawcett, J.P., Giles, G.I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4901149/
https://www.ncbi.nlm.nih.gov/pubmed/27331089
http://dx.doi.org/10.1016/j.dib.2016.05.037
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author Zadehvakili, B.
Giles, N.M.
Fawcett, J.P.
Giles, G.I.
author_facet Zadehvakili, B.
Giles, N.M.
Fawcett, J.P.
Giles, G.I.
author_sort Zadehvakili, B.
collection PubMed
description We have recently reported SAR data describing the pharmacological activity of a series of phenyl alkyl selenides and tellurides which catalyse the oxidation of thiols by hydrogen peroxide (H(2)O(2)), “The design of redox active thiol peroxidase mimics: dihydrolipoic acid recognition correlates with cytotoxicity and prooxidant action” B. Zadehvakili, S.M. McNeill, J.P. Fawcett, G.I. Giles (2016) [1]. This thiol peroxidase (TPx) activity is potentially useful for a number of therapeutic applications, as it can alter the outcome of oxidative stress related pathologies and modify redox signalling. This article presents data describing the molecular changes that occur to a TPx mimic upon exposure to H(2)O(2), and then the thiol mercaptoethanol, as characterised by UV–vis spectroscopy and HPLC retention time.
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spelling pubmed-49011492016-06-21 Data on the catalytic mechanism of thiol peroxidase mimics Zadehvakili, B. Giles, N.M. Fawcett, J.P. Giles, G.I. Data Brief Data Article We have recently reported SAR data describing the pharmacological activity of a series of phenyl alkyl selenides and tellurides which catalyse the oxidation of thiols by hydrogen peroxide (H(2)O(2)), “The design of redox active thiol peroxidase mimics: dihydrolipoic acid recognition correlates with cytotoxicity and prooxidant action” B. Zadehvakili, S.M. McNeill, J.P. Fawcett, G.I. Giles (2016) [1]. This thiol peroxidase (TPx) activity is potentially useful for a number of therapeutic applications, as it can alter the outcome of oxidative stress related pathologies and modify redox signalling. This article presents data describing the molecular changes that occur to a TPx mimic upon exposure to H(2)O(2), and then the thiol mercaptoethanol, as characterised by UV–vis spectroscopy and HPLC retention time. Elsevier 2016-05-24 /pmc/articles/PMC4901149/ /pubmed/27331089 http://dx.doi.org/10.1016/j.dib.2016.05.037 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Zadehvakili, B.
Giles, N.M.
Fawcett, J.P.
Giles, G.I.
Data on the catalytic mechanism of thiol peroxidase mimics
title Data on the catalytic mechanism of thiol peroxidase mimics
title_full Data on the catalytic mechanism of thiol peroxidase mimics
title_fullStr Data on the catalytic mechanism of thiol peroxidase mimics
title_full_unstemmed Data on the catalytic mechanism of thiol peroxidase mimics
title_short Data on the catalytic mechanism of thiol peroxidase mimics
title_sort data on the catalytic mechanism of thiol peroxidase mimics
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4901149/
https://www.ncbi.nlm.nih.gov/pubmed/27331089
http://dx.doi.org/10.1016/j.dib.2016.05.037
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