抗生素痢菌净与人血清白蛋白的相互作用

doi:10.3969/j.issn.0258-3283.2010.03.002

CORC > 北京大学 > 环境科学与工程学院

	抗生素痢菌净与人血清白蛋白的相互作用; Studies on the binding of antibiotic mequindox with human serum albumin
	曾舟华 ; 曾彩红 ; 周亚平 ; 曾昆 ; 徐振强 ; 刘义
刊名	化学试剂
	2010
关键词	痢菌净人血清白蛋白荧光猝灭荧光光谱紫外-可见吸收光谱 Mequindox(MEQ) Human serum albumin(HSA) Fluorescence quenching 3-dimensional fluorescence spectrum
DOI	10.3969/j.issn.0258-3283.2010.03.002
英文摘要	用荧光、同步荧光、三维荧光和紫外-可见吸收光谱法,研究了在生理条件下痢菌净(MEQ)与人血清白蛋白(HSA)相互作用的光谱学行为.分析了MEQ对HSA的荧光猝灭机制,计算了不同温度下的猝灭常数K_(SV)、结合常数K_b、结合位点数n、热力学参数(如:ΔH、ΔS、ΔG)和结合距离r,并探研了MEQ对HSA构象的影响.结果表明:MEQ对HSA荧光猝灭方式是动态猝灭;结合位点数<1;结合距离<4.2 nm;MEQ对HSA构象的影响不大.MEQ与HSA间结合作用较弱,作为肠、胃或体外消炎药时,不易被血清白蛋白储存和转运,药物在体内的残留量较少、残留时间较短、所产生的副作用也较小.; Fluorescence spectroscopy and UV-vis absorption spectroscopy were used to investigate the binding of antibiotic mequindox (MEQ) with human serum albumin (HSA) physiologically.The quenching mechanism of HSA with MEQ under fluorescence was discussed,results have indicated that it was a dynamic quenching process.Quenching constant K_(SV) and thermodynamic parameters,such as ΔH,ΔG,ΔS etc.at different temperatures were calculated.The binding was mainly driven by entropy and hydrophobic forces played a major role in the process.Distance between HSA and MEQ was 4.2 nm transfer.Furthermore,synchronous fluorescence spectroscopy and 3-dimensional fluorescence spectra were used to investigate molecular structure of HSA,with and without the existence of MEQ,results have indicated there was no structural change when considering experimental error.; 中文核心期刊要目总览(PKU); 中国科技核心期刊(ISTIC); 中国科学引文数据库(CSCD); 0; 3; 197-202,247; 32
语种	中文
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/242887]
专题	环境科学与工程学院
推荐引用方式 GB/T 7714	曾舟华,曾彩红,周亚平,等. 抗生素痢菌净与人血清白蛋白的相互作用, Studies on the binding of antibiotic mequindox with human serum albumin[J]. 化学试剂,2010.
APA	曾舟华,曾彩红,周亚平,曾昆,徐振强,&刘义.(2010).抗生素痢菌净与人血清白蛋白的相互作用.化学试剂.
MLA	曾舟华,et al."抗生素痢菌净与人血清白蛋白的相互作用".化学试剂 (2010).