Interaction Between Trans-resveratrol and Serum Albumin in Aqueous Solution

被引:37
作者
Cao, Shuhong [1 ]
Wang, Dandan [1 ]
Tan, Xiaoyan [1 ]
Chen, Jingwen [1 ]
机构
[1] Yancheng Inst Technol, Sch Chem & Biol Engn, Yancheng 224051, Peoples R China
关键词
Aqueous solution; Bovine serum albumin; Conformational change; Interaction; Trans-resveratrol; MULTI-SPECTROSCOPIC METHOD; BINDING; PROTEINS; FLUORESCENCE; CONFORMATION; FORCES; WATER; SITE; RATS;
D O I
10.1007/s10953-009-9439-7
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The interaction between trans-resveratrol (TR) with bovine serum albumin (BSA) in aqueous solution was investigated by means of fluorescence, synchronous fluorescence and infrared spectroscopy. The fluorescence of BSA can be quenched remarkably by TR in aqueous solution. A notable red-shift of the maximum emission of BSA from 340 to 353 nm together with appearance of an isoemissive point at 395 nm were observed. The results indicate that TR binds to BSA, forming a TR-BSA complex. The TR-BSA binding distance was determined to be less than 7 nm, suggesting that energy transfer from BSA to TR may occur. The interaction process is spontaneous. Based on the obtained thermodynamic parameters, electrostatic forces may play a major role in this process. Both synchronous fluorescence and FT-IR spectra confirmed the interaction, and indicate the conformational changes of BSA.
引用
收藏
页码:1193 / 1202
页数:10
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