Inhibition of tyrosinase by 4H-chromene analogs: Synthesis, kinetic studies, and computational analysis.
Edikarlos M BrasilLuciana M CanavieiraÉrica T C CardosoEdilene O SilvaJerônimo LameiraJosé L M NascimentoVera L Eifler-LimaBarbarella M MacchiDharmarajan SriramPaul V BernhardtJosé Rogério Araújo SilvaCraig M WilliamsCláudio Nahum AlvesPublished in: Chemical biology & drug design (2017)
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.