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Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study

2006; Elsevier BV; Volume: 126; Issue: 1 Linguagem: Inglês

10.1016/j.jlumin.2006.06.013

1872-7883

Yanqing Wang, Hongmei Zhang, Gencheng Zhang, Weihua Tao, Tang Shu-he,

Photochemistry and Electron Transfer Studies

The interaction between the flavonoid hesperidin and bovine serum albumin (BSA) was investigated by fluorescence and UV/Vis absorption spectroscopy. The results revealed that hesperidin caused the fluorescence quenching of BSA through a static quenching procedure. The hydrophobic and electrostatic interactions play a major role in stabilizing the complex. The binding site number n, and apparent binding constant KA, corresponding thermodynamic parameters ΔGo, ΔHo, ΔSo at different temperatures were calculated. The distance r between donor (BSA) and acceptor (hesperidin) was obtained according to fluorescence resonance energy transfer. The effect of Cu2+, Zn2+, Ni2+, Co2+, and Mn2+ on the binding constants between hesperidin and BSA were studied. The effect of hesperidin on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy and UV/Vis absorption spectroscopy.