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- W3115284229 abstract "Glutathione reductase (GR), which is a major antioxidant enzyme, is targeted in the treatment of many diseases due to the dual role of its product, reduced glutathione (GSH), in infected cells. This study's goal was to introduce new GR inhibitors to the literature. The inhibition profiles of the inhibitor were studied via two different approaches: in vitro and in silico. To this end, firstly, GR was isolated from human erythrocytes, following which the in vitro inhibition impacts of resorcinol derivatives and in silico inhibition mechanisms of them were elucidated. GR was obtained with a specific activity of 12.49 EU/mg protein and a 27.67% yield. Afterward, IC50 values was found to range from 0.014 to 1.500 mM. The docking studies of the compounds were performed against hGR receptors, and 4-hexylresorcinol had the lowest docking score of -4.276 kcal/mol. In conclusion, it was determined that 4-hexylresorcinol is the most effective inhibitor among resorcinol derivatives for human erythrocyte GR in accordance with both in vitro and in silico studies. 4-Hexylresorcinol may be utilized in drug design to target the recovery of GSH." @default.
- W3115284229 created "2021-01-05" @default.
- W3115284229 creator A5078731735 @default.
- W3115284229 date "2021-03-01" @default.
- W3115284229 modified "2023-10-17" @default.
- W3115284229 title "The In Vitro and In Silico Inhibition Mechanism of Glutathione Reductase by Resorcinol Derivatives: A Molecular Docking Study" @default.
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- W3115284229 doi "https://doi.org/10.1016/j.molstruc.2020.129790" @default.
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