Abstract
Xanthine oxidase (XO) has emerged as an important target for gout. In our previous study, salvianolic acid C (SAC) was found to show potent XO inhibitory activity, whereas the interaction mechanism was still not clear. Herein, an integrated approach consisting of enzyme kinetics, multi-spectroscopic methods and molecular docking was employed to investigate the interaction between SAC and XO. Consequently, SAC exhibited a rapid and mixed-type inhibition of XO with IC50 of 5.84 ± 0.18 μM. The fluorescence data confirmed that SAC presented a strong fluorescence quenching effect through a static quenching procedure. The values of enthalpy change, entropy change and Gibbs free energy change indicated that their binding was spontaneous and driven mainly by hydrophobic interactions. Analysis of synchronous fluorescence, circular dichroism and fourier transform infrared spectra demonstrated that SAC induced conformational changes of the enzyme. Besides, further molecular docking revealed that SAC occupied the catalytic center resulting in the inhibition of XO activity. This study provides a comprehensive understanding on the interaction mechanism of SAC on XO.
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