In silico identification and molecular mechanism of novel egg white-derived tyrosinase inhibitory peptides

This study aimed to identify novel tyrosinase inhibitory peptides from egg white proteins including ovalbumin, ovotransferrin and ovomucoid. Peptides GDVA and DEK were identified using computer-aided virtual screening and in vitro tyrosinase inhibition experiments. Especially, peptide DEK exhibited the strongest tyrosinase inhibitory capacity with IC50 value of 0.205 ± 0.07 mmol L−1. Molecular docking and isothermal titration calorimetry analysis (ITC) were performed to explore the molecular mechanism. The results revealed that two peptides interacted with key residues of tyrosinase mainly by hydrogen bonding and hydrophobic interaction. The binding reactions of these peptides with tyrosinase were spontaneous, endothermic and entropy driven. Furthermore, the structure of two peptide-tyrosinase complexes was compact and stable during the molecular dynamic simulation. These findings indicated that egg white-derived peptide DEK had potential as tyrosinase inhibitory peptide.