Eu(Ⅲ)、Cu(Ⅱ)对灯盏花素与BSA作用的扰动  

Interference of europium and copper ions on interaction between breviscapinun and bovine serum albumin

作　　者：张怀斌[1] 马丽英[1] 刘向勇[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：《化学试剂》2012年第12期1068-1072,共5页Chemical Reagents

基　　金：国家自然科学基金资助项目(60671010);山东省高等学校科技计划资助项目(J12LD55);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Eu(Ⅲ)、Cu(Ⅱ)对灯盏花素(Breviscapinun,BR)与牛血清白蛋白(Bovine serum al-bumin,BSA)作用的扰动。金属离子存在时BR对BSA的猝灭机制未发生改变,通过计算获得了二者相互作用的KA、n及热力学参数。结果表明,Cu(Ⅱ)的存在使得BR与BSA二者(BR-BSA)结合常数、结合位点数均增大,二者的作用力并未发生变化;而Eu(Ⅲ)存在时,BR-BSA作用的结合常数、结合位点数均减小,BR-BSA之间的作用力由疏水作用变为范德华力和氢键。从离子架桥作用、金属离子与BR的竞争作用,热力学参数的变化、配位化合物的形成等方面分析了影响BR-BSA作用的因素。The interference, caused by two ions （Eu^3＋, Cu^2＋ ） , on interaction between Breviscapinun （BR）and bovine serum albumin（BSA） was investigated by the fluorescence, absorption spectrum. The fluorescence quenching mechanism of BSA did not change in the presence of Eu3 ^＋ or Cu^2＋ ,and the binding constant （ KA ）, binding sites （n） and thermodynamic parameters （ AG, AH, AS） were obtained. The resuhs indicate that the binding constant, the binding site numbers of BR-BSA increased and the acting force did not change in the presence of Cu^2＋ . But the binding constant,binding site numbers of BR-BSA decreased and the acting force changed from hydrophobic interaction to Van der Waals＇ force or hydrogen bond in the presence of Eu3^＋. The analysis indicates that the interaction between BR and BSA was related to the metal ions function as the bridge ions,the competition role of metal ions, the change of thermodynamic parameters and the metal complex formation in Tris-HC1 medium（pH 7.40）.

关 键 词：灯盏花素 牛血清白蛋白 Eu(Ⅲ) Cu(Ⅱ) 结合作用 扰动 

分 类 号：O657.3[理学—分析化学]