Probing the Binding of the Flavonoid Diosmetin to Human Serum Albumin by Multispectroscopic Techniques
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- 作者：Guowen Zhang ; Lin Wang ; Junhui Pan
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：2012
- 出版时间：March 14, 2012
- 年：2012
- 卷：60
- 期：10
- 页码：2721-2729
- 全文大小：366K
- 年卷期：v.60,no.10(March 14, 2012)
- ISSN：1520-5118
文摘
The binding mechanism of molecular interaction between diosmetin and human serum albumin (HSA) in a pH 7.4 phosphate buffer was studied using atomic force microscopy (AFM) and various spectroscopic techniques including fluorescence, resonance light scattering (RLS), UV鈥搗is absorption, circular dichroism (CD), and Fourier transform infrared (FT鈥揑R) spectroscopy. Fluorescence data revealed that the fluorescence quenching of HSA by diosmetin was a static quenching procedure. The binding constants and number of binding sites were evaluated at different temperatures. The RLS spectra and AFM images showed that the dimension of the individual HSA molecules were larger after interaction with diosmetin. The thermodynamic parameters, 螖H掳 and 螖S掳 were calculated to be 鈭?4.56 kJ mol鈥? and 14.67 J mol鈥? K鈥?, respectively, suggesting that the binding of diosmtin to HSA was driven mainly by hydrophobic interactions and hydrogen bonds. The displacement studies and denaturation experiments in the presence of urea indicated site I as the main binding site for diosmetin on HSA. The binding distance between diosmetin and HSA was determined to be 3.54 nm based on the F枚rster theory. Analysis of CD and FT鈥揑R spectra demonstrated that HSA conformation was slightly altered in the presence of diosmetin.