Molecular docking studies of potent inhibitors of tyrosinase and α-glucosidase

Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Melanoma-specific anticarcinogenic activity has also been associated with this enzyme. Recently reported metabolites of tibolone exhibited significant inhibitory activities against both tyrosinase and α-glucosidase enzymes. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. It is comprehensively studied that the inhibition of α-glucosidase is crucial for glycemic control. The active site similarity between tyrosinase and α-glucosidase has also been observed. GOLD is utilized to investigate the conformation and binding affinities of newly discovered inhibitors. In both enzymes, metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Results obtained by recent study are not only consistent with the experimental findings but also provide a deeper insight into the structural attributes and overall molecular interactions.