摘要
采用荧光光谱技术,研究了不同温度下用于识别汞的荧光分子探针(WL-6)与生物大分子人血清白蛋白(HSA)的结合机理。结果表明,HSA在结合位点的荧光强度,随着WL-6的浓度增加而显著降低。根据荧光数据,得到了WL-6与HSA作用的结合常数、主要作用力及猝灭常数。从紫外吸收光谱、荧光光谱、同步荧光、三维荧光光谱和圆二色谱的结果可以看出,WL-6的结合改变了HSA的构象。
The binding mechanism of a fluorescent probe for Hg(WL-6) and biomacromolecule(human serum albumin, HSA) under different temperatures was studied by fluorescence spectroscopy. The results showed that the fluoresce intensity of HSA was significantly quenched by WL-6 with the increase of WL-6 concentration. The binding constants, the type of molecular force and the quench constants were obtained by the fluorescence intensity. The conformation of HSA was changed by the results of UV-vis, fluorescence spectra, synchronous fluorescence spectra, three-dimensional fluorescence spectra and circular dichroism(CD) spectra.
作者
陈昕
刘元艳
马明硕
陈杰
刘治刚
曾晓丹
CHEN Xin;LIU Yuanyan;MA Mingxu;CHEN Jie;LIU Zhigang;ZENG Xiaodan(Graduate School,Jilin Institute of Chemical Technology,Jilin 132022,China;Jilin Petrochemical Company Quality Inspection Center(Quality Inspection Workshop),Jilin 132022,China;Analysis and Test Center,Jilin Institute of Chemical Technology,Jilin 132022,China)
出处
《化工技术与开发》
CAS
2023年第3期1-6,共6页
Technology & Development of Chemical Industry
基金
吉林省科技厅项目(20220203020SF)
国家自然科学基金项目(51902125)。
关键词
荧光探针
人血清白蛋白
结合常数
binding constants
human serum albumin
binding site
