Molecular inhibitory mechanism of tricin on tyrosinase.

Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, Guangdong 510640, PR China.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy 2013 Apr 15

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Tricin was evaluated as a type of tyrosinase inhibitor with good efficacy compared to arbutin. Tricin functioned as a non-competitive inhibitor of tyrosinase, with an equilibrium constant of 2.30 mmol/L. The molecular mechanisms underlying the inhibition of tyrosinase by tricin were investigated by means of circular dichroism spectra, fluorescence quenching and molecular docking. These assays demonstrated that the interactions between tricin and tyrosinase did not change the secondary structure. The interaction of tricin with residues in the hydrophobic pocket of tyrosinase was revealed by fluorescence quenching; the complex was stabilized by hydrophobic associations and hydrogen bonding (with residues Asn80 and Arg267). Docking results implied that the possible inhibitory mechanisms may be attributed to the stereospecific blockade effects of tricin on substrates or products and flexible conformation alterations in the tyrosinase active center caused by weak interactions between tyrosinase and tricin. The application of this type of flavonoid as a tyrosinase inhibitor will lead to significant advances in the field of depigmentation. Copyright © 2013 Elsevier B.V. All rights reserved.

Citation

Yan Mu, Lin Li, Song-Qing Hu. Molecular inhibitory mechanism of tricin on tyrosinase. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. 2013 Apr 15;107:235-40