Rothnie Alice J
Life & Health Sciences, Aston University, Birmingham, B4 7ET, UK.
Methods Mol Biol. 2016;1432:261-7. doi: 10.1007/978-1-4939-3637-3_16.
Membrane proteins are localized within a lipid bilayer; in order to purify them for functional and structural studies the first step must involve solubilizing or extracting the protein from these lipids. To date this has been achieved using detergents which disrupt the bilayer and bind to the protein in the transmembrane region. However finding conditions for optimal extraction, without destabilizing protein structure, is time consuming and expensive. Here we present a recently-developed method using a styrene-maleic acid (SMA) co-polymer instead of detergents. The SMA co-polymer extracts membrane proteins in a small disc of lipid bilayer which can be used for affinity chromatography purification, thus enabling the purification of membrane proteins while maintaining their native lipid bilayer environment.
膜蛋白定位于脂质双分子层内；为了将它们纯化用于功能和结构研究，第一步必须涉及从这些脂质中溶解或提取蛋白质。迄今为止，这是通过使用去污剂来实现的，去污剂会破坏双分子层并与跨膜区域的蛋白质结合。然而，找到在不破坏蛋白质结构的情况下进行最佳提取的条件既耗时又昂贵。在此，我们介绍一种最近开发的方法，该方法使用苯乙烯-马来酸（SMA）共聚物代替去污剂。SMA共聚物在脂质双分子层的一个小圆盘内提取膜蛋白，该圆盘可用于亲和色谱纯化，从而能够在保持膜蛋白天然脂质双分子层环境的同时对其进行纯化。
