锌(Ⅱ)存在下灯盏花素与BSA相互作用的光谱分析  

The spectral analysis on interaction between breviscapinun and bovine serum albumin in the presence of Zn^(2+)

作　　者：张怀斌[1] 王雷[1] 刘向勇[1] 魏光成[1] 李怀祥[2] 

机构地区：[1]滨州医学院(烟台校区)药学院,山东烟台264003 [2]山东师范大学化学化工与材料科学学院,山东济南250014

出　　处：《分子科学学报》2012年第5期372-377,共6页Journal of Molecular Science

基　　金：国家自然科学基金资助项目(60671010);滨州医学院科研专项资助项目(BY2009KJ30)

摘　　要：运用荧光光谱、吸收光谱研究了灯盏花素(Breviscapinun,BR)与牛血清白蛋白(Bovine Serum Albumin,BSA)的相互作用.BR对BSA的荧光光谱具有猝灭作用,其猝灭机制为静态-动态联合猝灭,BSA发射峰蓝移.Zn2+的存在使得BSA发射峰蓝移程度降低,猝灭常数、结合常数、结合位点数减小.在较大浓度Zn2+存在下,BR与BSA作用的相关系数增大,猝灭机制变为静态猝灭.从Zn2+与BR的竞争作用,热力学参数的变化、配位化合物的形成3个方面分析了影响BR与BSA作用的因素.The interaction between Breviscapinun（BR） and bovine serum albumin（BSA） in the presence of Zn2＋ was investigated by the fluorescence,absorption spectrum.The fluorescence of BSA was quenched by BR,and the quenching mechanism of BSA was a static and dynamic quenching process.The maximum emission wavelength of BSA was blue-shift.When appropriate amount of Zn2＋ was added to the mixture of BSA and BR,a small blue-shift of the maximum emission wavelength of BSA was observed for BR,and the quenching constant,binding constant,binding sites decreased,and the correlation coefficient（R） increased.The quenching process of BSA was changed in the presence of Zn2＋.When the concentration of Zn2＋ was up to 1.0×10-4 mol·L-1,the quenching process was a static mechanism.The anaslysis indicates that the effect of Zn2＋ on the interaction between BR and BSA was related to the Zn2＋ competition role,the change of thermodynamic parameters and the Zn2＋ complex formation in Tris-HCl medium（pH=7.40）.

关 键 词：灯盏花素 牛血清白蛋白 Zn2+ 荧光光谱 

分 类 号：O657[理学—分析化学]