Wang Lu, Wan Yizhen, Ma Ning, Zhou Lele, Zhao Dongmin, Yu Jianning, Wang Huili, Lin Zhiping, Qian Weiping
State Key Laboratory of Bioelectronics, School of Biological Science and Medical Engineering, Southeast University, Nanjing 210096, China.
Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
Colloids Surf B Biointerfaces. 2022 Nov;219:112839. doi: 10.1016/j.colsurfb.2022.112839. Epub 2022 Sep 13.
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.
蛋白质相互作用的动力学和亲和力分析揭示了它们在生物过程中相关活动的信息。在此，我们通过自组装后190nm二氧化硅球的非凡光学干涉能力，建立了一个用于评估蛋白质A与二氧化硅胶体晶体（SCC）薄膜表面各种IgG物种之间相互作用的动力学和亲和力的系统。通过平衡朗缪尔模型和对时间依赖性数据的非线性最小二乘法分析来计算平衡缔合常数（KA）。相对蛋白质A/IgG结合亲和力为人类>兔>牛>山羊。此外，还研究并进行了不同种类IgG与蛋白质A在SCC薄膜界面处的竞争相互作用。这些发现可能有助于在多种传感器类型中使用蛋白质A和其他识别成分。此外，本研究可能提供一种确定球体颗粒表面蛋白质动力学和亲和力的新方法，这可能有助于推动球体颗粒在药物科学、生物医学工程和其他技术中的应用发展。
