Interactions between three polyphenols and bovine serum protein have been done in this study, which is aimed at providing the basis for the metabolism and transport of polyphenols in vivo. In this study, ultraviolet spectrophotometry, fluorescent spectrophotometry, circular dichroism spectroscopy and synchronous fluorescence spectrophotometry were used to analyze the relationship between isoorientin, ellagic acid, punicalagin and bovine serum albumin (BSA), respectively. The results showed that the fluorescence quenching mechanism of three polyphenols on BSA was mainly static quenching. And combining with three polyphenols, the conformation of BSA was changed. The binding ratio between isoorientin and BSA was approximately 2∶1, while the ratios between punicalagin, ellagic acid and BSA were both 1∶1. Isoorientin, punicalagin, ellagic acid interacted with BSA through hydrophobic force, and the combination of the three kinds of polyphenols and BSA was endothermal and entropy driven reaction. These results could provide theoretical support for the field of protein and polyphenol complexes.
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