摘要
本研究旨在对罗丹明类荧光探针ZM-6与人血清白蛋白(HSA)的相互作用进行研究。采用了荧光光谱法、三维荧光光谱法、同步荧光光谱法以及CD光谱法在模拟生理条件下对二者的相互作用以及HSA的构象进行了研究。研究结果表明,探针与ZM-6之间的猝灭机理主要是静态猝灭方式。根据热力学数据确定了二者之间的作用力,类型为范德华力和氢键。二者之间的结合距离为4.45 nm。同时得出,ZM-6对HSA的构象产生了影响。此研究对于探针分子的设计以及修饰提供有效的数据以及理论支持。
This study aimed to study the interaction between a Rhodiamin-based fluorescent probe ZM-6 and human serum albumin(HSA). The interaction between the two and the conformation of HSA were investigated by fluorescence spectrum, the three dimensional fluorescence spectrum, synchronous fluorescence spectrum and CD spectrum methods under simulated physiological conditions. The results revealed that the quenching mechanism between probe ZM-6 and HSA was mainly on static quenching. The thermodynamic parameters revealed that the binding of(ZM-6)-HSA was relied on Van der Waals force and hydrogen bond. The binding distance of ZM-6 with HSA was calculated to be 4.45 nm. The results demonstrated that the conformation of HSA was affected by ZM-6. This study could provide effective data and theoretical support for the design and modification of probe molecules.
作者
曾晓丹
马明硕
柳彩云
朱琳
Zeng Xiaodan;Ma Mingshuo;Liu Caiyun;Zhu Lin(Analysis and Test Center,Jilin Institute of Chemical Technology,Jilin,132022;School of Resources and Environment,University of Jinan,Jinan, 250022;School of Chemistry and Pharmaceutical Engineering,Jilin Institute of Chemical Technology,Jilin,132022)
出处
《基因组学与应用生物学》
CAS
CSCD
北大核心
2019年第1期129-134,共6页
Genomics and Applied Biology
基金
国家自然基金(21607053)
吉林市科技局(20166023
20156422)共同资助
关键词
探针
荧光
人血清白蛋白
结合常数
Probe
Fluorescence
Human serum albumin
Binding constants
