| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1230688 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2013 | 6 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Tricin effectively inhibits tyrosinase in a non-compatitive manner. ► Tricin quenches tyrosinase fluorescence by forming complex with tyrosinase. ► The tricin-enzyme complex is stabilized by hydrogen bonds and hydrophobic forces. ► A simulated model for the molecular interaction of tricin and tyrosinase.
