<i>In vitro and in silico</i> enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from <i>Vaccinium arctostapylous</i> L.

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 watersolubility 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 Cd2thorn, Cu2 thorn, Ni2thorn, Mg2 thorn 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 Ki 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 +/- 0.06mM, 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.

Journal

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS

Year

2022

Volume

40

Issue

22

Pages

11587-11593

ISSN

0739-1102

eISSN

1538-0254

DOI

10.1080/07391102.2021.1960893

WoS UID

WOS:000681536600001