期刊
JOURNAL OF LUMINESCENCE
卷 126, 期 1, 页码 211-218出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2006.06.013
关键词
hesperidin; bovine serum albumin; intrinsic fluorescence; binding thermodynamics; fluorescence resonance transfer
类别
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 K-A, corresponding thermodynamic parameters Delta G(o), Delta H-o, Delta S-o 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. (C) 2006 Elsevier B.V. All rights reserved.
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