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. .

限制的蛋白质（合成矩阵，例如溶胶 - 凝胶）作为一类材料具有 广泛的生物医学和生物技术的巨大潜在效用 申请。在大多数情况下，长期蛋白质稳定性具有保留率或 需要增强活动。充分利用 限制蛋白质，必须了解如何理解的生物物理机制 限制和共糖（即渗透液）调节相关蛋白质的特性。 拟议的项目建立在蛋白质动力学决定的日益认识的基础上 稳定性和反应性，这些功能上重要的蛋白质动力学又又是 由水合壳水显着调节。 拟议的项目将结合光谱，动力学和模拟。 基于确定分子生物物理学水平的方法，如何限制 存在和不存在渗透率改变水合壳的水相互作用以及如何 水合壳特性的这些改变在功能上影响重要的蛋白质 动力学。这一总体目标将通过两个具体的目标来实现： 具体目的1。确定在存在和不存在的情况下如何限制 渗透剂修饰了精选蛋白质和肽的水合壳水。 具体目的2。确定在存在和不存在的情况下如何限制 渗透剂会影响蛋白质动力学功能上重要的类别。 。