| Popis: |
Smilax china L. showed various biological activities mainly due to its phenolic components; however, the mechanism of isolated phenolic fraction against xanthine oxidase (XO) has not been investigated. Quercetin-3-O-rhamnoside (QORh) and chlorogenic acid (CGA) extracted from Smilax china L. ethyl acetate fraction was analyzed for its XO inhibitory kinetics and mechanism using multispectroscopic methods and molecular docking techniques. QORh and CGA reversibly inhibited XO activity in competitive and non-competitive modes, respectively. The bioactive compounds bound with XO were dominated mainly by hydrogen bonds and van der Waals forces to form QORh-XO, and CGA-XO complexes with one affinity binding site. The synchronous fluorescence, circular dichroism, three-dimensional (3D) fluorescence, and Fourier transform infrared spectra exhibited that XO binding with QORh or CGA leads to the secondary and tertiary structural variation of the protein. Additionally, molecular docking further revealed that QORh binds to the active site of XO and forms hydrogen coupling with amino acid residues. The results showed that QORh and CGA had inhibitory activity on XO, which might be further used to modify the bioactive compounds and improve their efficacy to treat gout. |
Full Text from ScienceDirect