酒石酸美托洛尔与牛血清蛋白相互作用的光谱研究  

Spectroscopic Research on the Interaction between Metoprolol Tartrate and Bovine Serum Protein

作　　者：俞波 兰秀风[1] 陈奇 

机构地区：[1]南京航空航天大学理学院,南京211106

出　　处：《西安文理学院学报（自然科学版）》2018年第1期81-85,共5页Journal of Xi’an University(Natural Science Edition)

基　　金：航空科学基金资助项目(20150352005);中央高校基本科研业务费专项资金资助项目(NS2015080)

摘　　要：运用荧光光谱对酒石酸美托洛尔与牛血清蛋白(BSA)之间的相互作用进行了研究.实验结果表明:酒石酸美托洛尔对BSA的内源荧光有较强的猝灭作用,猝灭机制为动态猝灭.测定了酒石酸美托洛尔与BSA在不同温度下的表观结合常数Ksv,Ksv分别为2.271×10~5、3.698×10~5、5.923×10~5.同时也测定了两种物质分子之间的结合常数与结合位点数,其中不同温度下酒石酸美托洛尔与BSA的结合位点数都约为1,说明酒石酸美托洛尔与BSA有单一的结合位点且受温度影响较小.在酒石酸美托洛尔与BSA的作用过程中反应的焓变ΔH>0、熵变ΔS>0,说明酒石酸美托洛尔与BSA之间的主要相互作用为疏水作用力;吉布斯自由能ΔG<0,表明结合过程是一个熵增加、吉布斯自由能降低的自发过程.In this paper, the interaction between metoprolol and bovine serum protein （BSA） was studied by fluorescence spectroscopy. The results showed that metoprolol tartaric acid had a strong quenching effect on the endogenous fluorescence of BSA, and the quenching mechanism was dynamic quenching. The apparent binding constant Ksv of metoprolol tartrate and BSA at different temperatures was measured, and Ksv were 2. 271 × 105 , 3. 698 × 105 and 5. 923 × 105 respectively. At the same time, the binding constants and the number of binding sites between the two material molecules are also measured. The binding sites of metoprolol tartrate and BSA were about 1 at different temperatures, indicating that metoprolol tartrate had a single binding site with BSA and was less affected by temperature. During the action of metoprolol tartrate and BSA, the enthalpy change of reaction is △H 〉 0 and entropy change △S 〉 0, indicating that the main interaction between metoprolol tartrate and BSA is hydrophobic interaction. The Gibbs free energy of AG is less than 0, indicating that the binding process is a spontaneous process of increasing entropy and reducing Gibbs＇s free energy.

关 键 词：生物医学光子学 酒石酸美托洛尔 牛血清白蛋白 荧光光谱 紫外吸收光谱 

分 类 号：O657.3[理学—分析化学] Q51[理学—化学]