Molecular simulation and tyrosinase inhibitory studies of arbutin-6′-undecenoate

Arbutin is frequently used as an inhibitor of tyrosinase, a key enzyme in the biosynthesis of melanin. Tyrosinase inhibitors are highly sought after by the pharmaceutical and cosmetic industries. Given the increasing interest in such products, we performed a one-step synthesis of acylated arbutin by protease-catalysed transesterification using undecylenic acid ester as acyl donor. We simulated the docking of tyrosinase with the product using AutoDock Vina and identified its activity as a tyrosinase inhibitor by in vitro assay against mushroom tyrosinase. We successfully synthesized arbutin-6′-undecenoate by the formation of an ester linkage between the carboxyl residue (C1″) of undecylenic acid ester and the C6′ glucose moiety of arbutin. Results showed that the binding affinity of arbutin-6′-undecenoate with tyrosinase was higher than that of arbutin. In addition, arbutin-6′-undecenoate inhibits tyrosinase activity effectively (IC50 = 0.16 mM). The results of this study strongly suggest that arbutin-6′-undecenoate is a promising candidate as tyrosinase inhibitor.