Encapsulation and Protein Stability

封装和蛋白质稳定性

• 批准号: 1607359
• 负责人: Gary Pielak
• 金额: $ 35.39万
• 依托单位: University of North Carolina at Chapel Hill
• 依托单位国家: 美国
• 项目类别: Standard Grant
• 财政年份: 2016
• 资助国家: 美国
• 起止时间: 2016-09-01 至 2019-08-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1607359&HistoricalAwards=false
• 关键词: Encapsulation; Protein; Stability

With this award, the Chemistry of Life Processes Program in the Chemistry Division funds Dr. Gary J. Pielak from the University of North Carolina-Chapel Hill for studies on how proteins behave when "confined" to small spaces. The term confinement refers to isolation of the protein in a cavity roughly the size of the protein itself. This is how many proteins find themselves when inside of cells. Such confinement can affect the behavior of proteins and enzymes. The project is determining how confinement affects protein behavior during synthesis, misfolding, turnover and transport. This information is important to industrial applications such as enzyme stabilization. This research is also expanding efforts to reach underrepresented undergraduates by teaming up with the UNC Scholars' Latino Initiative.This project is determining how confinement (isolation of the protein in a cavity roughly the size of the protein itself) affects protein behavior during synthesis, misfolding, turnover and transport. This information is important to industrial applications such as enzyme stabilization. The research is being accomplished by using a fluorine-labeled, metastable globular protein capable of reversible two-state folding that is entrapped in a unique system of reverse micelles. 19F NMR is being used to assess not only the free energy, but also the enthalpy and the entropy of unfolding. Structural effects of confinement also are being assessed.

有了这个奖项，化学部的生命过程化学项目资助了北卡罗来纳大学教堂山分校的加里J. Pielak博士研究蛋白质在“局限”于小空间时的行为。术语限制是指将蛋白质隔离在大致与蛋白质本身大小相同的空腔中。 这是多少蛋白质在细胞内找到自己。这种限制会影响蛋白质和酶的行为。该项目正在确定限制如何影响蛋白质在合成，错误折叠，周转和运输过程中的行为。这一信息对于酶稳定化等工业应用是重要的。这项研究还通过与美国学者协会的拉丁裔倡议合作，扩大了对代表性不足的本科生的影响。该项目正在确定限制（将蛋白质隔离在大致与蛋白质本身大小相同的空腔中）如何影响蛋白质在合成、错误折叠、周转和运输过程中的行为。这一信息对于酶稳定化等工业应用是重要的。这项研究是通过使用一种氟标记的亚稳态球状蛋白质来完成的，这种蛋白质能够可逆地进行两种状态的折叠，这种折叠被困在一种独特的反胶束系统中。19F NMR不仅用于评估自由能，还用于评估去折叠的焓和熵。限制的结构影响也正在评估中。