Copper containing tyrosinase enzyme is responsible for melanin biosynthesis in human. Anomalous growth of this enzyme causes hyper-pigmentation related disorders. Monophenols and Diphenols compounds are used as inhibitors and among these the some compounds exhibited significant inhibitory activities against the tyrosinase. Molecular docking studies of these enzymes with those metabolites have been the focus of this study. The active site of the tyrosinase is the two copper ions as binding site. The metal ions seem to play an important role in establishing the interaction within the cavity of active sites. Discovery Studio3.1 was utilized to investigate the conformation and binding affinities of our small molecules. The results indicate a possible mechanism for their anti-tyrosinase activity which may involve anability to chelate the copper atoms which are required for the catalytic activity of tyrosinase.
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