Tyrosinase plays determinant role in enzymatic browning of vegetables and fresh-cut fruits. Development of new tyrosinase inhibitors is of great concern in food and agriculture. To discover new inhibitors, novel phenolic derivatives were synthesized and their inhibitory effects were investigated on activity of mushroom tyrosinase. All compounds showed potent inhibitory activities in their low concentrations and compound 4-(4-hydroxyphenyl)butan-2-one (1b) was found to be the most potent inhibitor (73.75% inhibition, IC50 value 5.6 μmol L-1). This ligand inhibited enzyme activity in a mixed pattern and kinetic parameters were also determined. In vitro assays revealed that this compound has not cytotoxicity/hemolytic effects and can be considered as safe for further investigations. Analysis of fluorescence spectra showed that all ligands quenched enzyme intrinsic fluorescence. The quenching mode and important binding parameters were also calculated. Enzyme-ligands interactions were also theoretically analyzed by molecular docking and results showed that the ligands interact with structurally/functionally critical residues.
Keywords: Fluorescence quenching; Inhibition mechanism; Mixed inhibition; Molecular docking; Phenolic compounds; Tyrosinase inhibitor.
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