丁咯地尔与人血清白蛋白结合的光谱学研究  

Spectroscopic Investigation of the Interaction between Buflomedil and Human Serum Albumin

作　　者：杨锦艳[1] 王丽[1] 郑茂东[1] 张爱平[1] 

机构地区：[1]山西医科大学药学院,山西太原030001

出　　处：《分析测试学报》2009年第2期194-198,共5页Journal of Instrumental Analysis

基　　金：国家自然科学基金资助项目(20371031);山西高校科技研究开发项目(2007122)

摘　　要：用紫外吸收光谱法、荧光光谱法和傅立叶变换红外光谱法探讨了在模拟人体生理条件下,丁咯地尔与人血清白蛋白(HSA)的结合模式。结果表明:丁咯地尔对HSA的内源荧光有显著的猝灭作用,且猝灭机理主要为静态猝灭。丁咯地尔与HSA形成了1∶1的复合物,结合常数K=7.43×102L.mol-1(308 K)。根据F ster偶极-偶极非辐射能量转移机理,求得丁咯地尔与HSA间的结合距离r=2.64 nm。由热力学参数确定其作用力以氢键和范德华力为主。同步荧光和傅立叶变换红外光谱表明丁咯地尔对HSA二级结构的含量产生影响,使HSA的α-螺旋结构的含量明显降低,β-折叠和β-转角结构的含量增加。The binding model of buflomedil（BUF） and human serum albumin（HSA） has been investigated by UV absorption, fluorescence and FT - IR spectra under the simulative human physiological condition. The results showed that the intrinsic fluorescence of HSA was significantly quenched by BUF, in which the static quenching was the main model of fluorescence quenching. A complex of BUF -HSA was formed with molar ratio of I ： 1 and the binding constant of 7.43 × 10^2 L · mol^-1 at 308 K. A binding distance of 2.64 nm was obtained between BUF and HSA according to the theory of Foster＇s dipole -dipole non-radiation energy transfer mechanism. The hydrogen bond and van der Waals were proved to be the main binding force between BUF and HSA according to the corresponding thermodynamic parameters. The synchronous fluorescence and FT - IR spectra of BUF - HSA system also indicated that the presence of BUF would change the conformation and the secondary structure of HSA, in which the content of α-helix structure was decreased, while those of β-sheet and β-turn structure were increased.

关 键 词：丁咯地尔 人血清白蛋白 紫外光谱 荧光光谱 傅立叶变换红外光谱 

分 类 号：O657.3[理学—分析化学] R972.4[理学—化学]