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. .

受限蛋白质（在合成基质中，例如溶胶-凝胶）作为一类材料， 对广泛生物医学和生物技术具有重要的潜在效用 应用.在大多数情况下，长期蛋白质稳定性与保留或 需要加强活动。为了充分利用生物医学的影响， 限制蛋白质，这是至关重要的，以了解生物物理机制，如何 限制和共溶质（即渗压剂）调节相关的蛋白质性质。 拟议的项目是建立在越来越多的认识，蛋白质动力学决定 稳定性和反应性，这些功能上重要的蛋白质动力学反过来 由水化壳层沃茨显著调节。 拟议中的项目将使用光谱，动力学和模拟相结合的方法 基于分子生物物理学水平的方法来确定， 渗透剂的存在和不存在改变了水化壳水的相互作用， 水化壳性质的这些改变影响功能重要的蛋白质 动力学将通过两个具体目标来实现这一总体目标： 具体目标1。确定在存在和不存在添加剂的情况下 渗压剂修饰所选蛋白质和肽的水合壳沃茨。 具体目标2。确定在存在和不存在添加剂的情况下 渗透调节剂影响蛋白质动力学的重要功能类别。 .