Work

The mixed-type inhibition of tyrosinase by puerarin: Kinetics and computer simulation

Year: 2025

Type: article

Abstract: This paper uses inhibition kinetics, fluorescence spectroscopy, molecular docking, and molecular dynamics simulation to study how Puerarin (PUE) inhibits mushroom tyrosinase. Inhibition kinetics reveals that PUE inhibits tyrosinase in a reversible mixed-type manner with an IC 50 of 0.816 mmol/L and prefers binding to free tyrosinase. Fluorescence spectroscopy shows PUE binds spontaneously via static quenching with hydrophobic interactions as the main binding force and a single binding site. Synchronous and 3D fluorescence indicate PUE increases the microenvironment polarity of tyrosinase. Molecular docking confirms PUE can compete for the binding site and form a ternary complex. Molecular dynamics shows the tyrosinase/PUE complex is stable. In short, PUE inhibits tyrosinase by spontaneous binding in a reversible mixed-type manner. This characteristic provides theoretical support for its potential applications in the food industry, such as inhibiting browning and preserving fruits and vegetables, and in the cosmetics industry, such as serving as a natural whitening ingredient.

Source: Food Bioscience

DOI: 10.1016/j.fbio.2025.107972

Authors: Bo Ma, Rong Li, Feng Li, Xiao Hu, Yechuan Huang

Institutions: Southwest University of Science and Technology, Jingchu University of Technology

Language: English

Topic: melanin and skin pigmentation

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,380

Funder: Jingchu University of Technology