激光与光电子学进展, 2018, 55 (4): 043003, 网络出版: 2018-09-11
法莫替丁与牛血清蛋白相互作用的光谱研究 下载: 1636次
Spectroscopic Study on Interaction of Famotidine with Bovine Serum Albumin
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 spectroscopy biomedicine photonics famotidine fluorescence spectra bovine serum albumin ultraviolet absorption spectrum
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306 K和314 K下的表观结合常数K A,分别为9.861×10
4,3.891×10
4 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F rster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1.25 nm,发生了非辐射能量转移。
Abstract
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 KA of famotidine and BSA at 306 K and 314 K is determined to be 9.861×10
4 L/mol and 3.891×10
4 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 F rster nonradiative energy transfer theory, the interaction distance of famotidine and BSA is calculated to be 1.25 nm, and nonradiative energy transfer occurs.
俞波, 兰秀风, 张林, 邹如萍, 陈奇. 法莫替丁与牛血清蛋白相互作用的光谱研究[J]. 激光与光电子学进展, 2018, 55(4): 043003. Bo Yu, Xiufeng Lan, Lin Zhang, Ruping Zou, Qi Chen. Spectroscopic Study on Interaction of Famotidine with Bovine Serum Albumin[J]. Laser & Optoelectronics Progress, 2018, 55(4): 043003.