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

Abstract 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 IC 50 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.