光谱学与光谱分析 |
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Studies on the Interaction between Alpinetin and Human Serum Albumin by Fluorescence Spectroscopy |
ZHANG Guo-wen,WANG An-ping,JIANG Ting |
State Key Laboratory of Food Science and Technique, Nanchang University, Nanchang 330047, China |
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Abstract The interaction between alpinetin and human serum albumin (HSA) was studied by fluorescence and UV/Vis absorption spectroscopy. The results revealed that alpinetin caused the fluorescence quenching of HSA through a dynamic quenching procedure. The quenching constant was obtained at various temperatures. The binding locality was found to be an area 4.05 nm away from tryptophan residue in HSA based on Frster’s non-radiation energy transfer mechanism. The binding power between alpinetin and HSA is mainly the hydrophobic interaction according to the thermodynamic parameters. The effect of alpinetin on the conformation of HSA was analyzed by three-dimensional fluorescence spectra, contour spectra and synchronous spectra.
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Received: 2006-11-19
Accepted: 2007-02-26
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Corresponding Authors:
ZHANG Guo-wen
E-mail: gwzhang@ncu.edu.cn
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