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

使用噬菌体 T4 溶菌酶的合成结构稳定性突变体模拟竞争性蛋白质吸附

• 批准号: 9501842
• 负责人: Joseph McGuire
• 金额: $ 14.7万
• 依托单位: Oregon State University
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 1996
• 资助国家: 美国
• 起止时间: 1996-03-15 至 1998-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9501842&HistoricalAwards=false
• 关键词: Modeling; Competitive; Protein; Adsorption; Synthetic

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.

CTS-9501842约瑟夫·麦奎尔俄勒冈州立大学摘要该项目是当前研究的扩展，在该研究中，噬菌体T4溶菌酶的定点突变被用来探索吸附行为。所采用的实验技术包括原位椭偏测量、放射性标记和圆二色谱。以前用于分析单一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。这些模型允许在表面上有两种不同的蛋白质状态：一种是可交换的，另一种是不可交换的。该项目是对真实系统中蛋白质界面行为的多态机制建模的一次尝试。了解蛋白质在界面上的结构和作用对于开发生物分离技术、耐污染膜、生物兼容材料、生物传感器和相关应用具有重要意义。