荧光光谱法研究3-吡唑啉基叶绿素-a衍生物和牛血清白蛋白的相互作用  

Study on Interaction Between 3-Pyrrolinyl Chlorophyll-a Derivatives and Bovine Serum Albumins by Fluorescence

作　　者：刘淑燕[1] 刘春林[1] 刘永明[2] 王进军[2] 刘振波[2] 

机构地区：[1]烟台大学药学院,山东烟台264005 [2]烟台大学化学生物理工学院,山东烟台264005

出　　处：《烟台大学学报（自然科学与工程版）》2008年第1期29-34,共6页Journal of Yantai University(Natural Science and Engineering Edition)

基　　金：山东省教育厅资助项目(200391006008)

摘　　要：用荧光光谱法、同步荧光光谱、紫外-可见分光光度法研究3-吡唑啉卟吩f-2甲酯(Mf2-5)、3-吡唑啉卟吩f-3甲酯(Mf3-5)与牛血清白蛋白(BSA)的相互结合反应.实验表明Mf2-5、Mf3-5与牛血清白蛋白的相互结合作用为静态猝灭过程,在溶液中二者以物质的量之比1∶1牢固结合,25℃时其结合反应的平衡常数分别为:KMf2-5=6.14×105L.mol-1,KMf3-5=1.02×105L.mol-1.根据F rster非辐射能量转移机理,求算了给体(BSA)与受体(Mf2-5、Mf3-5)间距离r和能量转移效率E分别为:rMf2-5=4.48 nm,rMf3-5=4.86 nm,EMf2-5=0.24,EMf3-5=0.20.并推测了二者之间的主要作用力为疏水作用力.The binding reaction between 3-pyrrolinyl chlorophyll-a derivatives （Mf2-5 ,Mt3-5 ） and bovine serum albumins （BSA） is studied by fluorescence spectra, synchronous fluorescence spectra, and UV-Vis absorption spectra. The research results indicate that the combination reaction of them is a single static quenching process, and Mr2-5 or Mf3-5 strongly bounds BSA with the molar ratio of 1 ： 1 and the binding equilibrium constant Ko at 25 ℃ is KMf2-5 =6.14 ×10^5L·mol^-1, KMf3-5 = 1.02×10^5L·mol^-1. The shortest binding distance r and the energy transfer efficiencies E between donor BSA and acceptor of Mf2-5 or Mf3-5 are obtained by Forster nonradiative energy transfer mechanism as follows： rMf-5 =4. 48 nm, rMf3-5 = 4. 86 nm, EMf2-5 =0.24 ,EMf3-5 =0.20. The main sort of binding force between them is speculated about to be hydro phobic force.

关 键 词：牛血清白蛋白 荧光猝灭 结合反应 

分 类 号：O644.17[理学—物理化学]