The in vitro and in silico inhibition mechanism of glutathione reductase by some small molecules

Reduced glutathione (GSH), a product of the antioxidant glutathione reductase (GR), has a dual function in affected cells and is thus a therapeutic target for many diseases. The purpose of this investigation was to include new GR inhibitors in the current scientific literature. Some modifications were made to the original coumarin structure, and a docking research against the enzyme was performed in this investigation. Here, the standard coumarin structure was modified and bound to an enzyme using the Molegro Virtual Docker software. Docking experiments were performed on the crystal structure of human glutathione reductase (PDB ID: 2GH5). Template values for coumarin isotopes ranged from -158.567 to 109.516. The degree of affinity for the enzyme glutathione reductase. The results indicate that with a little tweaking, coumarin derivatives can be used to effectively block the enzyme Glutathione Reductase. In this study, eight complexes were used, and one of these complexes The Cu (S1M-S2) molecule 2 inhibited the GR enzyme, to put it another way. At an IC50 value of 7.92168 µM, Cu(S1M-S2)2 was shown to inhibit the GR enzyme, and 3D interaction maps between the two were shown.