Abstract
Piceatannol (PIC) displays a wide spectrum of biological activities, such as antioxidation, antibacterial activity and anti-inflammation, but the biochemical and molecular mechanism is not fully understood. In this study, the interaction of PIC with bovine serum albumin (BSA) was studied by fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, circular dichroism spectroscopy and molecular simulation. The effects of PIC on BSA non-enzymatic glycosylation, fibrillation, thermal stability, and structure information were also studied. The results showed that the formation of PIC-BSA complex by mainly hydrogen-bonding forces resulted in the conformational changes of protein. PIC inhibited the formation of β-sheets structures of BSA. BSA still maintained the esterase-like good activity in the presence of PIC. In addition, PIC significantly reduced the degree of BSA glycosylation. These results provided a basis for the molecular interaction between PIC and protein, and suggested the potential effect of PIC in preventing the progression of diabetes mellitus.
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