Some anticancer agents as effective glutathione S-transferase (GST) inhibitors

Abstract

Abstract The objective of this research was to investigate the impact of anthraquinone (AQ) compounds on the activity of the enzyme glutathione S-transferase (GST). The interaction between GST and some AQs (alizarin, purpurin, quinizarin, and dantron) was investigated, and IC50 and K i levels were determined for each compound. The results obtained reveal that these compounds are potent GST inhibitors. K i values of these compounds against GST were found ranging from 9.133 ± 0.895 to 36.992 ± 6.194 μM. In the in vitro study, purpurin was identified as the most potent AQ against GST. Thereafter, binding mode exploration of purpurin to the enzyme was undertaken to elucidate its mechanism of action. To this end, molecular docking was conducted. According to the docking results, purpurin can bind to the enzyme and form a stable complex. Together with this, binding potential of purpurin was less than the standard ligand. Examination of both the inhibitory activity in vitro and molecular docking interactions of these anticancer agents with GST, an enzyme important for detoxification metabolism, led to the identification of important relationships between these compounds and GST. The findings may offer structural direction for developing superior anticancer drugs or powerful GST inhibitors.