Inhibition of Xanthine Oxidase by Four Phenolic Acids: Kinetic, Spectroscopic, Molecular Simulation, and Cellular Insights.

ABSTRACT: The inhibition mechanism and binding properties of four phenolic acids (ferulic acid (FA), p-coumaric acid (CA), gallic acid (GA), and protocatechuic acid (PA)) on xanthine oxidase (XOD) were investigated. All four phenolic acids acted via a mixed inhibition pattern, mainly influencing the hydrophobic regions and secondary conformation of XOD through hydrophobic bonding and hydrophobic association. Molecular dynamics simulations exhibited that the complexes of XOD with FA and CA revealed smaller radii of gyration (Rg) and solvent-accessible surface areas (SASA), along with lower variability in root-mean-square deviation (RMSD) and root-mean-square fluctuation (RMSF), collectively indicating greater structural stability. FA, CA, and PA significantly reduced uric acid (UA) concentrati

SUBMITTER: Wang X 

PROVIDER: S-EPMC12523838 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature