Selenium chelating collagen peptides as tyrosinase inhibitor: Structure characterization and inhibitory activity

Organoselenium compounds have garnered significant attention as a pivotal tyrosinase inhibitor. In this study, we explore a novel collagen peptides-selenium chelate (CP-Se) for tyrosinase inhibitory activity. The results show that selenium can be mainly bound to N─H and C ═ O bonds on collagen peptides. The IC₅₀ value of tyrosinase inhibitory activity for the CP-Se is 0.47 mg/mL, which demonstrates a significant reduction compared to collagen peptides. Furthermore, the CP-Se exhibits low cytotoxicity, with a survival rate of 93.04 ± 1.48%. The CP-Se effectively curtails melanin production to 55.89 ± 1.12% and intracellular tyrosinase activity to 65.21 ± 2.39%, showcasing its efficacy in mitigating pigmentation processes. Additionally, the CP-Se is found to bind specifically to tyrosinase at the critical residues (Asn 81, His 244, or Arg 268), which are pivotal in facilitating the inhibition of tyrosinase activity. Conclusively, a novel approach to reducing the biological toxicity associated with selenium has been developed, while simultaneously amplifying the tyrosinase inhibitory activity of collagen peptides. This would provide a robust theoretical underpinning for the advancement of novel tyrosinase inhibitors.