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

CTS-9501842 约瑟夫·麦奎尔俄勒冈州州立大学 摘要 该项目是目前研究的延伸，其中噬菌体T4溶菌酶的定点突变体用于探测吸附行为。 所采用的实验技术包括原位椭圆偏振法、放射性标记和圆二色性。 简单的动力学模型，以前用于分析单一的蛋白质吸附数据将扩展到顺序和竞争吸附的蛋白质。 该模型允许表面上的两种不同的蛋白质状态：一种可交换的和一种不可交换的。 该项目是一个尝试，以模拟蛋白质界面行为的多状态机制在真实的系统。 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非常重要。

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.