Synthetic Polymer Nanoparticles as an Abiotic Artificial Inhibitor of Tyrosinase

An innovative methodology is presented for synthesizing synthetic polymer nanoparticles (TINPs) as potent tyrosinase inhibitors. This inhibition strategy combines the integration of two distinct functionalities, phenol, and phenylboronic acid, within the TINPs structure. The phenyl group mimics the natural monophenol substrate, forming a strong coordination with the catalytic copper ion, significantly inhibiting tyrosinase activity. Additionally, phenylboronic acid interacts with catechol, another tyrosinase substrate, further reducing enzyme efficiency. The shared benzene ring in phenyl and phenylboronic acid enhances binding to tyrosinase's hydrophobic pocket near its copper active site, contributing to potent inhibition. TINPs exhibit exceptional performance, boasting an impressive IC50 value of 3.5x10-8 m and an inhibition constant of 9.8x10-9 m. Validation of the approach is unequivocally demonstrated through the successful inhibition of tyrosinase activity and melanin production, substantiated in both in vitro and in vivo scenarios. The mechanism of TINP inhibition is elucidated through circular dichroism and Fourier transform infrared spectroscopy. This study introduces a versatile design approach for developing abiotic polymer-based enzyme inhibitors, expanding possibilities in enzyme inhibition research. Synthetic polymer nanoparticles (TINPs) is created as potent tyrosinase inhibitors, incorporating phenol and phenylboronic acid components. TINPs demonstrate exceptional performance with an IC50 value of 3.5x10-8 m and an inhibition constant of 9.8x10-9 m. Validated in vitro and in vivo, the inhibition mechanism is elucidated using circular dichroism and Fourier transform infrared.image