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The molecular structure properties-binding affinity relationship of a series of flavonoids and bovine serum albumin (BSA) was investigated in vitro from comparing the binding constants determined through the fluorescence method. As a result, the binding process was greatly influenced by different structural elements or substituents of flavonoids under analysis. The hydroxylation at the positions C3, C6, C4', C5' (for type I) and C5, C3' (for type II) were in favor of forming hydrogen bonds with the amino acids of BSA, which was of great
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