Inhibition of Tyrosinase by 4H-Chromene Analogues: Synthesis, Kinetic Studies and Computational Analysis
- Brasil, Edikarlos M.
- Canavieira, Luciana M.
- Cardoso, Érica T. C.
- Silva, Edilene O.
- Lameira, Jeronimo
- Nascimento, Jose L. M.
- Eifler-Lima, Vera L.
- de Matos Macchi, Barbarella
- Sriram, Dharmarajan
- Bernhardt, Paul V.
- Silva, Jose Rogerio Araujo
- Williams, Craig M.
- Alves, Claudio N.
DOIAbstract
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 4μM, 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
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