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| - Important Role of the 3-Mercaptopropionamide Moiety inGlutathione: Promoting Effect on Decomposition of the Adduct ofGlutathione with the Oxoammonium Ion of TEMPO
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| - Cyclic voltammetry of TEMPO in aqueous 0.1 M NaOH in the presence of glutathione (GSH) orcysteine (Cys) indicated the following points: (i) Both of the thiols rapidly formed adducts 3 withoxoammonium ion 1 anodically generated from TEMPO. (ii) 3 generated from GSH entered asucceeding reaction that generated n-oxide anion 2- (the reduced TEMPO). (iii) 3 produced fromCys remained intact over the time scale of voltammetry. A structural feature of GSH was consideredto contribute to the observed behavior of this tripeptide. Possible structural features were evaluatedby screening various thiols on the basis of whether they provided GSH-like voltammetric results.The 3-mercaptopropionamide group with an amide hydrogen in GSH was determined to beresponsible for the observed difference between GSH and Cys. The likely function is to transform3 from GSH into a 5-imino-1,2-oxathiolane intermediate, thereby releasing 2-. Product analysisfor reactions of model thiols representing GSH and Cys with 1 provided support for this argumentand suggested that the reaction of GSH or Cys with 1 would produce the corresponding disulfides,regardless of whether a five-membered ring intermediate was formed. The proposed function ofthe 3-mercaptopropionamide moiety of GSH may provide useful insight for the molecular designof exogenous thiol compounds as novel drugs for the treatment of GSH-depletion-related disorders.
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