Molecular Docking and In Silico ADMET Study Reveals Flavonoids as a Potential Inhibitor of Aromatase

Background: Aromatase is an enzyme that plays a critical role in the development of estrogen receptor positive breast cancer. As aromatase catalyses the aromatization of a drostenedione to estrone, a naturally occurring estrogen, it is a promising drug target for therapeutic management. Objective: The objective of the present study is to evaluate the binding interaction of flavonoid compounds with cytochrome P450 enzyme aromatase and also checked ADME/T properties of best scored compounds. Methods: To examine different molecules for this purpose, test ligands like Flavonoids derivatives were docked against our target protein aromatase enzyme retrieved from protein data bank (PDB Id: 3S7S), considering Exemestane as the positive control. Results: Docking results revealed that, with respect to their free binding energy 6B, 6K, 4K and 2K compounds have the lowest binding energy compared to positive control. In silico ADME/T predictions revealed that all best scored compounds had good absorption as well as solubility characteristics. Conclusion: The present findings provided valuable information on the binding process of flavonoid compounds to the binding site of aromatase. These compounds may serve as potential lead compounds for developing new aromatase inhibitors in breast cancer treatment.