Evaluation of inhibitory effects of some novel phenolic derivatives on the mushroom tyrosinase activity: Insights from spectroscopic analyses, molecular docking and in vitro assays

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-hydrox-yphenyl)butan-2-one (1b) was found to be the most potent inhibitor (73.75% inhibition, IC50 value 5.6 mu mol 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

Automated summary

This study investigated the inhibitory effects of novel phenolic derivatives on the activity of mushroom tyrosinase. The compounds showed potent inhibitory activities at low concentrations, with compound 1b exhibiting the highest inhibitory effect. The compound was found to have a mixed pattern of enzyme inhibition, and in vitro assays showed it to be non-cytotoxic. Analysis of fluorescence spectra revealed that all ligands quenched the enzyme's intrinsic fluorescence. Molecular docking analysis further supported the interaction between the ligands and critical residues of the enzyme.