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适应性脂膜模拟系统用于膜蛋白的溶液NMR研究

Chih-Ta Henry Chien¹, Lukas R Helfinger¹, Mark J Bostock¹

¹Department of Biochemistry, University of Cambridge , 80 Tennis Court Road, Cambridge CB2 1GA, U.K.

Journal of the American Chemical Society

|October 10, 2017

概括

我们开发了一种可调节的纳米粒子系统,使用saposin-A (SapA) 和脂质来研究用溶液NMR进行的膜蛋白 (MPs). 这种方法可以进行接近原生膜蛋白的分析,包括G蛋白结合受体.

科学领域:

生物化学
结构生物学
生物物理

背景情况:

膜蛋白 (MPs) 对于细胞功能至关重要,但由于它们的疏水性质,研究它们具有挑战性.
溶液核磁共振 (NMR) 光谱是一种用于蛋白质原子层结构和动态分析的强大技术.
现有的MP结构确定方法往往难以维持与原生环境相似的环境.

研究的目的:

开发一个可调整尺寸的,基于脂的膜模拟系统,用于溶液中膜蛋白的NMR研究.
证明该系统在接近原生条件下分析膜蛋白的适用性.
使用溶液NMR研究多种膜蛋白,包括G蛋白合受体.

主要方法:

使用sapsin-A (SapA) 支架蛋白制造Salipro纳米粒子.
通过在pH范围内调整sapsin-to-lipid静态度来调整Salipro纳米粒子大小.
在SapA-dimyristoylphosphatidylcholine纳米颗粒中加入三种代表性膜蛋白,包括G蛋白合受体.
使用溶液NMR光谱分析内置的膜蛋白.

主要成果:

证明了基于SapA的Salipro系统在膜蛋白研究中的适用性.
通过改变素与脂质的比率来调整纳米粒子大小的能力.
成功保持足够的脂含量以模仿本地膜环境.
实现多重膜蛋白的溶液核磁共振分析,包括G蛋白结合受体.

结论:

开发的适应尺寸的Salipro纳米粒子系统对于膜蛋白的溶液NMR研究是有效的.
这种系统为在接近原生条件下研究膜蛋白提供了一个多功能平台.
调节纳米颗粒大小的能力有助于通过溶液NMR研究广泛的膜蛋白.

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