pH荧光分子探针与人血清白蛋白之间相互作用的研究  

Study on Interaction between the pH Fluorescent Molecule Probe and Human Serum Albumin

作　　者：尹玉 姜懿珊 陈昕 陈杰 YIN Yu;JIANG Yi-shan;CHEN Xin;CHEN Jie(Center of Characterization and Analysis,Jilin Institute of Chemical Technology,Jilin Jilin 132022;Institut Franco-chinois del'Energie Nucléaire,Sun Yat-sen University,Guangdong Zhuhai 519000,China)

机构地区：[1]吉林化工学院分析测试中心,吉林吉林132022 [2]中山大学中法核工程与技术学院,广东珠海519000

出　　处：《广州化工》2024年第9期86-88,共3页GuangZhou Chemical Industry

基　　金：国家自然基金(No:21607053)。

摘　　要：在模拟生理条件下,用光谱法研究了pH荧光探针WZK-33与人血清白蛋白(HSA)的相互作用机制。由光谱谱图结果可以得出,此探针可以猝灭HSA的荧光,探针与HSA之间的猝灭机制主要是静态猝灭方式。由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,结合位点为一个。二者之间的结合距离为4.77 nm。同步荧光、三维荧光光谱以及CD光谱表明探针改变了HSA的构象。The binding of pH fluorescent probe(WZK-33)with human serum albumin(HSA)in physiological buffer(pH=7.40)was investigated by the multispectroscopic technique.Spectroscopic analysis revealed that the probe could quench the fluorescence of HSA and the quenching mechanism between probe WZK-33 and HSA was static quenching.The calculated thermodynamic parameters revealed that the binding of WZK-33-HSA was relied on Van der Waals forces and hydrogen bond and the number of binding site was to be one.The binding distance of WZK-33 with HSA was calculated to be 4.77 nm.The results of synchronous fluorescence spectra,three-dimensional fluorescence spectra and CD spectra demonstrated that the conformation of HSA was changed by the binding of WZK-33.

关 键 词：荧光探针 人血清白蛋白 结合常数 结合位点 

分 类 号：O657.39[理学—分析化学]