Cu^(2+)对香豆素与BSA相互作用的影响  

Effect of Cu^(2+) on the Interaction Between Bovine Serum Albumin and Coumarin

作　　者：刘雪锋 方云 

机构地区：[1]江南大学化学与材料工程学院,江苏无锡214036

出　　处：《江南大学学报（自然科学版）》2005年第6期645-648,共4页Joural of Jiangnan University (Natural Science Edition)　

基　　金：江苏省自然科学基金项目(BK2004019);江南大学自然科学预研基金项目(2004LYY019)资助课题

摘　　要：采用荧光光谱法研究了Cu2+对香豆素类中药有效成分的母核化合物香豆素与牛血清白蛋白(BSA)相互作用的影响.实验结果表明,有Cu2+存在时,香豆素对BSA内源荧光的猝灭过程是以静态猝灭为主,香豆素与BSA结合过程的表观结合常数KA数值为104量级,结合位点数n的范围为2.9~3.4,香豆素-BSA的分子间相互作用力类型仍是以疏水作用为主,熵增加是该作用过程的主要热力学驱动因素;与不含Cu2+的相比,香豆素对BSA内源荧光的静态猝灭常数KP、表观结合常数KA都明显增大,但结合位点数和分子间作用力类型没有明显改变,表明Cu2+可能参与了香豆素与BSA的结合过程.The effect of Cu^2＋ on the interaction between bovine serum albumin （BSA） and coumarin was investigated mainly by means of fluorescence spectroscopy. The experimental results showed that in the presence of Cu^2＋ , the type of BSA intrinsic fluorescence quenching by coumarin is mainly static quenching. The magnitude of the apparent association constant KA in coumarin-BSA binding process is about 10^4 and the number of binding sites of coumarin on BSA is within the range of 2. 9～3. 4. The main driving force in coumarin-BSA interactional process is hydrophobic force, thereby the increase in entropy is the primary thermodynamic driving factor. While compared with those parameters in the absence of Cu^2＋, the static quenching constant （Kp） and Ka are higher than those in absence of Cu^2＋ , however, the number of binding sites of coumarin on BSA and the main driving force in coumarin-BSA binding process are not changed evidently. Therefore, it is estimated that Cu^2＋ is likely to participate in the interaction between coumarin and BSA.

关 键 词：CU^2+ 香豆素 牛血清白蛋白 相互作用 荧光光谱 

分 类 号：O657[理学—分析化学]