Colla corii asini–derived peptides as tyrosinase inhibitors: identification, inhibitory activity and molecular mechanism

Abstract

SummaryThe aim of the present study was to investigate the effect of peptides derived from Colla corii asini on tyrosinase. The sequences of Colla corii asini–derived peptides were identified using mass spectrometry. To characterise the potential peptides with tyrosinase inhibitory activity and clarify their molecular mechanism, both in silico digestion and molecular docking were used. In addition, the tyrosinase inhibitory activities of potential peptides in vitro were also validated. The results showed that Colla corii asini consisted of 472 peptides, and most peptides derived from collagen. Peptides DGGR, DGD, NAGE, LVGE and GSEG were released from the digestion of Colla corii asini‐derived peptides and possessed potent inhibitory activity against tyrosinase with IC50 values of 0.92, 0.50, 0.77, 0.66 and 0.69 mg mL−1, respectively. The molecular interaction results showed that hydrogen bond and van der Waals interactions are important forces in the interaction of peptides with tyrosinase. Surface forces containing aromatic interaction, hydrogen bond, hydrophilicity and solvent‐accessible surface contributed to the interaction between tyrosinase and peptides.