法莫替丁与牛血清蛋白相互作用的光谱研究  

Spectroscopic Study on Interaction of Famotidine with Bovine Serum Albumin

作　　者：俞波 兰秀风[1] 张林[2] 邹如萍 陈奇 Yu Bo;Lan Xiufeng;Zhang Lin;Zou Ruping;Chen Qi(School of Science, Nanjing University of Aeronautics ＆ Astronautics, Nanjing, Jiangsu 210016, China;School of Science, Hohai University, Nanjing, Jiangsu 211100, China)

机构地区：[1]南京航空航天大学理学院,江苏南京210016 [2]河海大学理学院,江苏南京211100

出　　处：《激光与光电子学进展》2018年第4期397-403,共7页Laser & Optoelectronics Progress

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

摘　　要：法莫替丁是组织胺H2受体拮抗剂,具有减弱胃酸生成的作用。通过分析荧光光谱和紫外可见吸收光谱探寻了法莫替丁与牛血清蛋白(BSA)的猝灭作用,并阐明两者间的作用机制。通过分析可知,法莫替丁能有效猝灭BSA的内源荧光,猝灭机制为静态猝灭。测定了法莫替丁与BSA在306K和314K下的表观结合常数KA,分别为9.861×104,3.891×104 L/mol。通过对猝灭过程中的热力学参数进行分析,得出法莫替丁与BSA的作用力主要是氢键和范德瓦耳斯力。凭借F9rster非辐射能量转移理论计算得到了法莫替丁和BSA的相互作用距离为1.25nm,发生了非辐射能量转移。Famotidine is a histamine H2 receptor antagonist, which has a significant inhibitory effect on gastric acid secretion. The quenching effect between famotidine and bovine serum albumin （BSA） is studied with the analysis of fluorescence spectrum and ultraviolet visible absorption spectrum, and the interaction mechanism between them is elucidated. The results show that famotidine has strong quenching effect on the endogenous fluorescence of BSA, and the quenching mechanism is static quenching. The apparent binding constant Kn of famotidine and BSA at 306 K and 314 K is determined to be 9. 861 × 104 L/mol and 3. 891 × 104 L/mol. The calculated thermodynamic parameters show that the interaction between famotidine and BSA is mainly hydrogen bond and van der Waals force. According to the F6rster nonradiative energy transfer theory, the interaction distance of famotidine and BSA is calculated to be 1.25 nm, and nonradiative energy transfer occurs.

关 键 词：光谱学 生物医学光子学 法莫替丁 荧光光谱 牛血清白蛋白 紫外吸收光谱 

分 类 号：O657.3[理学—分析化学]