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Updated: Jan 15, 2026

Biochemical Measurement of Neonatal Hypoxia
Published on: August 24, 2011
Inhibition of Xanthine Oxidase by Four Phenolic Acids: Kinetic, Spectroscopic, Molecular Simulation, and Cellular
Xiao Wang1, Di Su2, Xinyu Luo1
1Crop Breeding and Cultivation Research Institution, Research Center for Agricultural Products Preservation and Processing, Shanghai Academy of Agricultural Sciences, Shanghai 201403, China.
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) concentration in the 25-100 μM range. Although GA only reduced UA levels in cell models at 25 μM, this effect was likely due to its larger polar surface area, which limits cellular uptake. Absorption, distribution, metabolism, excretion, and toxicity (ADMET) evaluation suggested that these phenolic acids have potential for development.
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