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灯盏花素与牛血清白蛋白相互作用的荧光光谱研究
引用本文:张怀斌,马丽英,荣先国.灯盏花素与牛血清白蛋白相互作用的荧光光谱研究[J].化学研究,2012(2):13-16.
作者姓名:张怀斌  马丽英  荣先国
作者单位:滨州医学院烟台校区药学院,山东烟台264003
基金项目:滨州医学院科研专项资助项目(BY2009KJ30).
摘    要:采用荧光光谱法和紫外吸收光谱法研究了灯盏花素(BR)与牛血清白蛋白(BSA)的相互作用;利用热力学方程计算了295K和308K下的热力学参数ΔH、ΔG和ΔS,根据Stern-Volmer方程求出了猝灭常数和结合常数.结果表明,BR对BSA的荧光具有猝灭作用,其猝灭机制为动态-静态联合猝灭,BSA发射峰略有蓝移.BR与BSA之间的作用力主要为疏水作用.

关 键 词:灯盏花素  牛血清白蛋白  相互作用  荧光光谱

Interaction between breviscapine and bovine serum albumin studied by fluorescence spectrometry
ZHANG Huai-bin,MA Li-ying,RONG Xian-guo.Interaction between breviscapine and bovine serum albumin studied by fluorescence spectrometry[J].Chemical Research,2012(2):13-16.
Authors:ZHANG Huai-bin  MA Li-ying  RONG Xian-guo
Affiliation:(Pharmaceutical College, Binzhou Medical University, Yaitai 264003, Shandong, China)
Abstract:The interaction between breviscapine (BR) and bovine serum albumin (BSA) was in- vestigated by means of fluorescence spectrometry and ultraviolet absorption spectrometry. The thermodynamic parameters AH, AG and AS at 295 K and 308 K were calculated using thermo- dynamic equations. The quenching constant, binding constant and binding sites were obtained according to Stern-Volmer equation. Results indicate that the fluorescence of BSA is quenched by BR, and BR functions to quench the fluorescence of BSA by a static-and-dynamic joint quenching process, with the maximum emission wavelength of BSA being slightly blue-shifted. Besides, the interaction between BR and BSA is dominated by hydrophobic force.
Keywords:breviscapine  bovine serum albumin  interaction  fluorescence spectrometry
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