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The intermolecular interaction between isoliquiritigenin (ISL) and bovine serum albumin (BSA) under imitated physiological conditions was investigated using fluorescence, circular dichromism (CD) and molecular docking methods. The results revealed that the fluorescence quenching of BSA at 338nm by ISL resulted from the formation of ISL–BSA complex. The number of binding sites (n) for ISL binding on...
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