Abstract
In this study, xanthine oxidase was immobilized for the first time using a novel magnetic metal-organic framework material (Fe3O4-SiO2-NH2@MnO2@ZIF-8-NH2). A ligand fishing method was established to rapidly screen XOD inhibitors from Ligusticum wallichii based on the immobilized XOD. Characterization and properties of the immobilized enzyme revealed its excellent stability and reusability. A ligand was screened from Ligusticum wallichii and identified as ligustilide by ultra-high performance liquid chromatography tandem mass spectrometry. The IC50 value of ligustilide was determined to be 27.70 ± 0.13μM through in vitro inhibition testing. Furthermore, molecular docking verified that ligustilide could bind to amino acid residues at the active site of XOD. This study provides a rapid and effective method for thepreliminary screening of XOD inhibitors from complex natural products and has great potential for further discovery of anti-hyperuricemic compounds.
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