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.