Modeling Competitive Protein Adsorption with Synthetic, Structural Stability Mutants of Bacteriophage T4 Lysozyme

摘要该项目是当前噬菌体T4溶菌酶位点定向突变体用于探测吸附行为的研究的延伸。实验技术包括原位椭偏、放射性标记和圆二色性。以前用于分析单个蛋白质吸附数据的简单动力学模型将扩展到蛋白质的顺序和竞争吸附。该模型允许表面有两种不同的蛋白质状态：一种是可交换的，一种是不可交换的。该项目试图模拟真实系统中蛋白质界面行为的多状态机制。了解蛋白质在界面上的结构和作用对于生物分离技术、抗污染膜、生物相容性材料、生物传感器和相关应用的发展至关重要。

CTS-9501842 Joseph McGuire Oregon State University ABSTRACT The project is an extension of current research in which site-directed mutants of bacteriophage T4 lysozyme are used to probe adsorption behavior. Experimental techniques employed include in situ ellipsometry, radiolabeling and circular dichroism. Simple kinetic models previously used to analyze single protein adsorption data will e extended to sequential and competitive adsorption of proteins. The models allow two distinct protein states on the surface: one exchangeable and one non-exchangeable. The project is an attempt to model multi-state mechanisms of protein interfacial behavior in real systems. Understanding the structure and role of proteins at interfaces is important in the development of bioseparations technology, fouling-resistant membranes, biocompatible materials, biosensors and related applications.