Homology in the Binding Patterns of Human and Rat Androgen Receptors with various Ligands

Scientists routinely use in-vivo animal experiments to study the reproductive and endocrine effects of various chemicals in humans. Rats are being used as the most suitable animal model for such investigations. Use of animal models to envisage the mode of action of a particular chemical in humans is questionable unless we can explain the binding similarities. In this study, an in-silico docking was employed to visualise if androgens and their agonists bind with androgen receptors of humans and rats in a similar pattern using BIOVIA Discovery Studio 2018. Amino acid residues involved in bond formation, nature of bonding, LibDock score and bond distances were calculated to compare the binding affinities. It was found that ASN 705, GLN 711, ARG 752 and THR 877 were the major amino acid residues in hydrogen bonding of selected ligands with both human and rat androgen receptors. Thus, the present study answers numerous questions that may arise while selecting rats as laboratory animal models to validate the androgenic effects of chemicals in humans.