CORC  > 厦门大学  > 化学化工-已发表论文
荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用; Interaction of 1-Hydroxypyrene with BSA Using Fluorescence Anisotropy and Synchronous Fluorescence Analysis Methods
张静 ; 陈薇晓 ; 张唯 ; 段滢 ; 朱玉秀 ; 朱亚先 ; 张勇
2015-08-10
关键词荧光各向异性 1-羟基芘 牛血清白蛋白 结合常数 构型变化 作用方式 Fluorescence anisotropy 1-Hydroxypyrene(1-OHP) Bovine serum albumin(BSA) Binding constant Conformation change Interaction mode
英文摘要在模拟生理条件下,应用荧光各向异性法研究了多环芳烃(PAHS)代谢标志物1-羟基芘(1-OHP)与牛血清白蛋白(bSA)的相互作用,并结合同步荧光法研究作用过程中bSA的构型变化,初步探讨了二者的结合方式.研究结果表明,1-OHP与bSA有较强的结合作用,形成1∶1复合物,平均结合平衡常数为3.63x106l/MOl,且其结合作用强弱随着bSA浓度大小发生变化.1-OHP可与bSA的色氨酸残基结合,使bSA构型发生变化,进而使色氨酸残基周围环境的疏水性降低.; Fluorescence anisotropy was employed to investigate the interaction of 1-hydroxypyrene( 1-OHP),the metabolism biomarker of PAHs in vivo,with a model transport protein of bovine serum albumin( BSA)under simulated physiological conditions.Combined with synchronous fluorescence spectra,the conformation transition of BSA was also investigated.The experiment results showed that 1-OHP can bind to BSA strongly and a 1 ∶ 1 complex was formed,with an average binding equilibrium constant of 3.63×106L / mol.Also as the amounts of BSA differ,the interaction of 1-OHP and BSA was dominated by strong and weak binding modes alternately.Moreover,1-OHP can bind to tryptophan residues and induce the conformational and microenvironmental changes of BSA,increasing the tryptophan residue of BSA exposuring to a less hydrophobic micro-environment.; 国家自然科学基金(批准号:21075102;21177102); 中央高校基本科研业务费专项资金(批准号:2013121052); 国家级大学生创新创业项目基金(批准号:DC2013035)资助~~
语种zh_CN
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/107247]  
专题化学化工-已发表论文
推荐引用方式
GB/T 7714
张静,陈薇晓,张唯,等. 荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用, Interaction of 1-Hydroxypyrene with BSA Using Fluorescence Anisotropy and Synchronous Fluorescence Analysis Methods[J],2015.
APA 张静.,陈薇晓.,张唯.,段滢.,朱玉秀.,...&张勇.(2015).荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用..
MLA 张静,et al."荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用".(2015).
个性服务
查看访问统计
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。


©版权所有 ©2017 CSpace - Powered by CSpace