دورية أكاديمية
Diselenoamino acid derivatives as GPx mimics and as substrates of TrxR: in vitro and in silico studies.
| العنوان: | Diselenoamino acid derivatives as GPx mimics and as substrates of TrxR: in vitro and in silico studies. |
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| المؤلفون: | Sudati JH; Universidade Federal do Pampa (Unipampa), Dom Pedrito, RS, Brazil., Nogara PA, Saraiva RA, Wagner C, Alberto EE, Braga AL, Fachinetto R, Piquini PC, Rocha JBT |
| المصدر: | Organic & biomolecular chemistry [Org Biomol Chem] 2018 May 23; Vol. 16 (20), pp. 3777-3787. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101154995 Publication Model: Print Cited Medium: Internet ISSN: 1477-0539 (Electronic) Linking ISSN: 14770520 NLM ISO Abbreviation: Org Biomol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Cambridge, UK : Royal Society of Chemistry, c2003- |
| مواضيع طبية MeSH: | Computer Simulation*, Biomimetic Materials/*chemistry , Biomimetic Materials/*metabolism , Glutathione Peroxidase/*metabolism , Organoselenium Compounds/*chemistry , Organoselenium Compounds/*metabolism , Thioredoxin-Disulfide Reductase/*metabolism, Animals ; Catalytic Domain ; Male ; Models, Molecular ; Molecular Docking Simulation ; Oxidation-Reduction ; Rats ; Thioredoxin-Disulfide Reductase/chemistry |
| مستخلص: | Excessive production of reactive species in living cells usually has pathological effects. Consequently, the synthesis of compounds which can mimic the activity of antioxidant enzymes has inspired great interest. In this study, a variety of diselenoamino acid derivatives from phenylalanine and valine were tested to determine whether they could be functional mimics of glutathione peroxidase (GPx) and substrates for liver thioredoxin reductase (TrxR). Diselenides C and D showed the best GPx mimicking properties when compared with A and B. We suppose that the catalytic activity of diselenide GPx mimics depends on the steric effects, which can be influenced by the number of carbon atoms between the selenium atom and the amino acid residue and/or by the amino acid lateral residue. Compounds C and D stimulated NADPH oxidation in the presence of partially purified hepatic mammalian TrxR, indicating that they are substrates for TrxR. Our study indicates a possible dissociation between the two pathways for peroxide degradation (i.e., via a substrate for TrxR or via mimicry of GPx) for compounds tested in this study, except for PhSeSePh, and the antioxidant activity of diselenoamino acids can also be attributed to their capacity to mimic GPx and to be a substrate for mammalian TrxR. |
| المشرفين على المادة: | 0 (Organoselenium Compounds) EC 1.11.1.9 (Glutathione Peroxidase) EC 1.8.1.9 (Thioredoxin-Disulfide Reductase) |
| تواريخ الأحداث: | Date Created: 20180509 Date Completed: 20190304 Latest Revision: 20190304 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1039/c8ob00451j |
| PMID: | 29737350 |
| قاعدة البيانات: | MEDLINE |
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