Protein Reactivity in Sol-Gel Matrices: Hydration Effects in Confined Spaces

溶胶-凝胶基质中的蛋白质反应性：密闭空间中的水合效应

• 批准号: 7937773
• 负责人: JOEL M FRIEDMAN
• 金额: $ 33.2万
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-30 至 2011-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7937773
• 关键词: Address; Arts; Biomedical Engineering; Biotechnology; Cations; Confined Spaces; Coupled; Drug Formulations; Encapsulated; Environment; Foundations; Gel; Glass; Goals; Hand; Hemeproteins; Hemoglobin; Hydration status; Hydrogels; Investigation; Kinetics; Knowledge; Liquid substance; Membrane Proteins; Methodology; Modification; Molecular; Motion; Play; Process; Property; Protein Dynamics; Proteins; Protocols documentation; Reaction; Relaxation; Research; Role; Series; Side; Solutions; Solvents; Structure; Structure of molecular layer of cerebellar cortex; System; Techniques; Testing; Urea; Water; aqueous; base; design; insight; interfacial; novel strategies; polyol; simulation; sugar

Confined proteins (in synthetic matrices, e.g. sol-gels) as a class of materials have significant potential utility for a broad range of biomedical and biotechnology applications. In most situations, long-term protein stability with either retention or enhancement of activity is required. To fully harness the biomedical implications of confined proteins, it is essential to understand the biophysical mechanisms of how confinement and co-solutes (i.e. osmolytes) modulate the relevant protein properties. The proposed project is built on the growing realization that protein dynamics determine stability and reactivity and that these functionally important protein dynamics are in turn significantly modulated by hydration shell waters. The proposed project will use a combination of spectroscopic, kinetic and simulation based approaches to determine on a molecular biophysics level, how confinement in the presence and absence of osmolytes alters hydration shell water interactions and how these alterations in hydration shell properties impact functionally important protein dynamics. This overall objective will be pursued through two specific aims: Specific aims 1. Determine how confinement in the presence and absence of added osmolytes modifies hydration shell waters of select proteins and peptides. Specific aims 2. Determine how confinement in the presence and absence of added osmolytes impacts functionally important categories of protein dynamics. .

限域蛋白质（在合成基质中，例如溶胶-凝胶）作为一类材料具有 在广泛的生物医学和生物技术领域具有巨大的潜在效用 应用程序。在大多数情况下，保留或保留蛋白质的长期稳定性 需要加强活动。充分利用生物医学影响 受限蛋白质，了解其生物物理机制至关重要 限制和共溶质（即渗透剂）调节相关的蛋白质特性。 拟议的项目是建立在人们日益认识到蛋白质动力学决定的基础上的 稳定性和反应性，这些功能重要的蛋白质动力学反过来又 受水合壳水的显着调节。 拟议的项目将结合光谱、动力学和模拟 基于分子生物物理学水平的方法来确定如何限制 渗透剂的存在和不存在会改变水合壳水相互作用以及如何改变 水合壳特性的这些变化影响功能重要的蛋白质 动力学。这一总体目标将通过两个具体目标来实现： 具体目标 1. 确定在存在或不存在添加物的情况下如何进行限制 渗透调节剂可改变特定蛋白质和肽的水合壳水。 具体目标 2. 确定在存在或不存在添加物的情况下如何进行限制 渗透调节剂影响蛋白质动力学的功能重要类别。 。