利福平与人血清白蛋白作用的荧光光谱  

Fluorescence Spectroscopy Study of Humen Serum Albumin Quenched by Rifampicin Capsules

作　　者：陈晓波[1] 康栋国[1] 李崧[1] 赵承易[1] 陈晓珊[1] 丁焕平[1] 

机构地区：[1]北京师范大学分析测试中心应用光学北京重点实验室,北京100875

出　　处：《光谱学与光谱分析》2006年第4期674-677,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金项目;教育部留学回国人员科研启动基金资助项目

摘　　要：蛋白质是一类重要的生物大分子,它不仅是构成细胞内原生质的主要成分,也是生命现象的物质基础。对于蛋白质的探索是最复杂的课题之一。以荧光光谱为手段,文章研究了药物利福平(Rifampicin cap-sules)与人血清白蛋白(HSA)的作用,测量发现利福平和人血清白蛋白的色氨酸残基的结合位置为R=2.567 nm,临界距离R0为2.433 nm。利福平-HSA的Lineweaver-Burk猝灭曲线的离解常数Kd=19.42×10-6mol.L-1且结合常数Ks=5.149×104L.mol-1。It is obvious that the albumin is a kind of important large biophysical molecular. The albumin is the main component of plasma within cell. It is also the matter basis of life phenomenon. The fluorescence spectroscopy of humen serum albumin（HSA） and the interaction of HSA and the rifampicin capsules （lfp） were studied. When the rifampicin capsules （lfp） was added into HSA solution gradually, an interesting new phenomenon emerged in emission spectrum The combination constant of rifampicin capsules（lfp） is about Ks =5. 149× 10^4 L·mol^-1, and the dissociation constant is about Kd=19. 42× 10^-6 mol·L^-1. The quenching process of rifampicin capsules（lfp）-HSA is not dynamic quenching, which resulted from the molecular diffusion and collision. That is the static quenching process resulting from the chemical component between molecules. The energy transfer efficiency between rifampicin capsules（lfp） and HSA is E=0. 42. According to these calculation results, the combination position between the binding site of rifampicin capsules（lfp） and the tryptophane of HSA is about R=2. 567 nm. The critical dis tance, when transfer efficiency equals 50%, is about R0 =2. 433 nm.

关 键 词：利福平 荧光猝灭 人血清白蛋白 

分 类 号：O657.3[理学—分析化学]