In Silico Study Highlighting the Interactions Between the Active Sites of Steroidogenic Enzymes and Endocrine Disruptors Found in Daily Use Products

Abstract

Endocrine-disrupting chemicals (EDC) mimic steroid hormones; they can get easily bonded with enzymes even if their affinity is somewhat similar to natural reactants of the respective enzyme, forming subsequent hormones. This study aims to show the interactions between the active sites of key steroidogenic enzymes and endocrine disruptors. The main method used to reach the objective was molecular docking to study the relationship between the receptors and ligands and the binding affinity between EDC and Steroidogenic enzymes' active site amino acids. Molecular docking was also performed between the natural reactants of steroidogenesis and their respective steroidogenic enzymes so that a comparison could be made between the binding affinities of endocrine-disrupting chemicals and natural reactants with the respective steroidogenic enzymes. All the EDCs showed an affinity for the active site amino acids of key steroidogenic enzymes. Triclosan showed the highest affinity with the lowest binding energy required for all three key steroidogenic enzymes, while nitrate had the lowest affinity with the highest binding energy required. In comparison with the affinities showed by the reference reactants, all the EDCs studied show low affinities. Still, since EDCs tend to accumulate in the tissues, as their amount increases, it would surpass the reference reactants and would bind more efficiently, leading to endocrine disruption. © 2024 by the authors.