Phosphoglycerate mutase 1 (PGAM1) is an important glycolytic enzyme that plays a significant role in cancer metabolism. It catalyzes the conversion of 3-phosphoglycerate (3-PG) to 2-phosphoglycerate (2-PG), facilitating energy release during glycolysis. PGAM1 is often upregulated in various cancers, including breast, lung, and prostate cancers, contributing to tumor growth and progression by coordinating glycolysis and anabolic processes which makes it an appealing target for drug development. In this study, we screened drugs, food, and natural compound libraries against PGAM1 by using structure based virtual screening approach. A total of 100 compounds from each library were screened and then docked to find the best plausible modes of the hits. Based on the binding affinities, 5 compounds from each library were selected for molecular interactions analysis. After analyzing the interactions, the top compound from each library was subjected to 200 ns simulation to check the effect of hits on the protein. The simulation results revealed that the hits made stable interactions with the protein during simulation and no confirmational changes were observed in the structure of protein. All these findings suggest that the selected compounds can serve as lead compounds in inhibiting the biological activity of PGAM1, but it requires further experimental investigation.
Alanzi et al. (Fri,) studied this question.