Inhibition of tyrosinase by 4H‐chromene analogs: Synthesis, kinetic studies, and computational analysis

Inhibition of mushroom tyrosinase was observed with synthetic dihydropyrano[3,2‐b]chromenediones. Among them, DHPC04 displayed the most potent tyrosinase inhibitory activity with a Ki value of 4 μm, comparable to the reference standard inhibitor kojic acid. A kinetic study suggested that these synthetic heterocyclic compounds behave as competitive inhibitors for the L‐DOPA binding site of the enzyme. Furthermore, molecular modeling provided important insight into the mechanism of binding interactions with the tyrosinase copper active site. An inhibitory study involving development of new compounds with Tyrosinase activity by using experimental and computational techniques.