动力学
球体
蛋白质-蛋白质相互作用
胶体
平衡常数
化学
生物物理学
胶体二氧化硅
受体-配体动力学
化学工程
材料科学
纳米技术
物理化学
生物
生物化学
物理
量子力学
天文
工程类
涂层
作者
Lu Wang,Yizhen Wan,Wei Wang,Lele Zhou,Dongmin Zhao,Jianning Yu,Huili Wang,Zhiping Lin,Weiping Qian
标识
DOI:10.1016/j.colsurfb.2022.112839
摘要
Kinetic and affinity analysis of protein interactions reveals information on their related activities in biological processes. Herein, we established a system for evaluating the kinetics and affinity of the interaction between protein A and various IgG species on the surface of silica spheres of silica colloidal crystal (SCC) films by the extraordinary optical interference capabilities of 190 nm silica spheres after self-assembly. The equilibrium association constant (KA) was calculated by the equilibrium Langmuir model and nonlinear least-squares analysis of time-dependent data. The relative protein A/IgG binding affinity is human > rabbit >cow >goat. In addition, the competitive interaction of distinct species of IgG with protein A at the interface of SCC films was studied and performed. These findings may help with the use of protein A and other recognition components in a number of sensor types. Furthermore, this research might offer a novel approach to determining the kinetics and affinity of proteins on the surface of spheres particles, which may contribute to the development of the application of spheres particles in pharmaceutical science, biomedical engineering, and other techniques.
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