Inhibitory Effect of Quercetin on Tyrosinase and Its Molecular Mechanism
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Abstract:
The type and intensity of the inhibitory effect of quercetin on tyrosinase were studied using enzyme inhibition kinetics with L-dopa as a substrate. The type of fluorescence quenching, binding sites, and the type of interaction between quercetin and tyrosinase were analyzed using fluorescence spectroscopy. Furthermore, the molecular mechanism of the inhibitory effect was investigated using flexible molecular docking. The results showed that quercetin inhibited the activity of tyrosinase with an inhibitor constant (KI) of 36 mM. Quercetin can be regarded as a competitive and reversible inhibitor of tyrosinase. Quercetin bound to the active site of tyrosinase via hydrophobic interactions and hydrogen bonds at a ratioof 1 : 1, and quenched the fluorescence of tyrosinase by static quenching. Concomitantly, molecular docking results confirmed that quercetin occupied the active site of tyrosinase and formed strong hydrogen bonds with residues Asn260 and Gly62 located at the active site of tyrosinase. Moreover, hydrophobic interaction played a key role in stabilizing the structure of the complex formed.
