MOLECULAR INSIGHTS INTO TOXIN-ENZYME INTERACTIONS: DOCKING STUDIES ON CYP1A2 (2HI4) AND GST (1GTA): AN IN-SILICO APPROACH

Abstract

This study applies molecular docking methods to predict interactions of environmental toxins with two vital human detoxification enzymes, cytochrome P450 1A2 and glutathione S-transferase. Through simulation of the binding dynamics of environmental toxins to these enzymes, the aim is the prediction of binding affinities, potential inhibitory activities, and detoxification efficiencies. Docking simulation results show that some toxins exhibit high binding affinities at the active sites of CYP1A2 and GST, suggesting potential competitive inhibition or metabolic transformation. For instance, benzo[a]pyrene-like compounds exhibit high interactions with CYP1A2, suggesting potential metabolic activation or inhibition, while other environmental toxins exhibit favourable binding to GST, suggesting efficient detoxification pathways. These findings emphasize the applicability of molecular docking in the prediction of toxicological effects of environmental toxins and the efficacy of enzymatic detoxification processes. Such computational tools may be applicable in the risk assessments and guide the development of measures to limit toxin exposure. Future studies should aim to relate these in silico observations with experimental verifications to advance our understanding on toxin-enzyme interactions and their implications to human health.