In vitro and in silico enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from Vaccinium arctostapylous L
| Autor: | Ercan Bursal, Neslihan Balcı, Halis Şakiroğlu, Fikret Türkan |
|---|---|
| Přispěvatelé: | Belirlenecek |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Evolution
In silico Metal ions in aqueous solution metals chemicals chemistry.chemical_compound molecular docking Structural Biology GST enzyme Acid Variability Molecular Biology chemistry.chemical_classification biology Capacity Chemistry General Medicine Glutathione biology.organism_classification In vitro inhibition Vaccinium arctostapylous L Enzyme inhibition Glutathione S-transferase Enzyme Biochemistry Liver biology.protein Vaccinium |
| Popis: | Glutathione s-transferase (GST) is a class of enzymes that performs a wide array of biological functions. However, GST enzymes are most famously known for their roles in catalyzing the conjugation of reduced glutathione (GSH) to electrophilic centers on a wide variety of substrates to induce water-solubility to compounds as a protective antioxidant mechanism against toxic substances. In the present study, in vitro inhibition effects of coumarin, ascorbic acid, sodium sulfide, sodium azide, citric acid compounds, and Cd2+, Cu2+, Ni2+, Mg2+ metal ions against GST enzyme were determined. For this aim, the GST enzyme was purified from Vaccinium arctostapylous L. using the glutathione-agarose affinity chromatography and Sephadex G-100 gel filtration steps. The respective metals and chemical compounds were used at different concentrations for measuring their in vitro GST activity effects. The K-i values of these agents were determined as 0.450 +/- 0.13, 15.05 +/- 7.05, 0.009 +/- 0.001, 0.022 +/- 0.006, 0.120 +/- 0.36, 0.150 +/- 0.06, 0.223 +/- 0.03, 0.002 +/- 0.0003, and 0.136 +/- 0.06 mM, respectively. Finally, the molecular docking interactions of the compounds with the GST target enzyme were evaluated using Autodock Tools-1.5.6. The effective molecular interactions of coumarin, citric acid, ascorbic acid, and sodium sulfide with GST target enzyme were found with their binding lowest energy affinities -4.62, -3.04, -2.53, and -1.67 kcal/mol, respectively. Communicated by Ramaswamy H. Sarma |
| Databáze: | OpenAIRE |
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