Real-Time Profiling of Anti-(Epithelial Cell Adhesion Molecule)-Based Immune Capture from Molecules to Cells Using Multiparameter Surface Plasmon Resonance

Real-Time Profiling of Anti-(Epithelial Cell Adhesion Molecule)-Based Immune Capture from Molecules to Cells Using Multiparameter Surface Plasmon Resonance
复制标题

使用多参数表面等离子共振实时分析从分子到细胞的基于抗(上皮细胞粘附分子)的免疫捕获

DOI:
10.1021/acs.langmuir.8b03898
复制
发表时间:
2019
期刊:
影响因子:
3.9
通讯作者:
Lu Qinghua
Lu Qinghua
中科院分区:
化学2区
文献类型:
--
作者:
Gao Su;Chen Shuangshuang;Lu Qinghua

文献摘要

相似文献

Antibodies of epithelial cell-adhesion molecule (anti-EpCAM)-based interfaces have proven to be highly efficient at capturing circulating tumor cells (CTCs). To achieve the bonding of anti-EpCAM to the interface, biotin and streptavidin are used to modify the surface. These processes are critical to subsequent cell-capture efficiencies. However, quantitative research on the interactions between biotin, streptavidin, and biotinylated anti-EpCAM on the interface is lacking. In this work, the thermodynamics and kinetics of biomolecular interactions were determined by using surface plasmon resonance. The equilibrium binding affinities for biotinylated anti-EpCAM to streptavidin and streptavidin to biotin (illustrated by biotin-PEG400-thiol) were found to be 2.75 × 106and 8.82 × 106M–1, respectively. Each streptavidin can bind up to 2.30 biotinylated anti-EpCAM under thermodynamic equilibrium. The findings provide useful information to optimize the modification of anti-EpCAM and improve the capture efficiency of CTCs.