Edible bird's nest peptide (EBNP) with high whitening activity: Sequences analysis, whitening activity characterization and molecular docking study

At present, more and more researchers found that peptides have strong physiological activity. In this study, the effects of Edible bird's nest peptide (EBNP) on whitening were investigated in vitro and in vivo . It was found that EBNP reduced melanin content and inhibited tyrosinase activity of B16 cells and zebrafish in a concentration-dependent manner. Additionally, EBNP significantly down-regulated the expression of MITF, TYR, TYRP1 and TYRP2 genes in B16 cells at 500 μg/mL ( p < 0.05) and the expression of MITF and TYR genes in zebrafish at 50 μg/mL ( p < 0.05). After the zebrafish was treated with EBNP (50 μg/mL), the expression of MITF and TYR genes was down-regulated by 61.51 % and 87.00 %, respectively. Molecular docking showed that peptide FRAF mainly bound to MITF, TYR, TYRP1 and TYRP2 proteins by hydrogen bonds and electrostatic interactions. These results suggested that EBNP was a promising whitening material for food, skin care and pharmaceutical industries. EBNP showed excellent effect on anti-melanogenesis and tyrosinase activity inhibition in vitro and in vivo . It was due to that EBNP down-regulated the expression of melanogenic genes and the peptide FRAF in EBNP could bind to melanogenic proteins. • EBNP reduced the melanin content in vivo and in vitro . • EBNP inhibited tyrosinase activity in vivo and in vitro . • EBNP down-regulated the expression of melanogenesis related genes. • Peptide FRAF of EBNP could bind to melanogenesis related proteins.