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用于膜蛋白稳定化的新型二甲苯连接麦芽糖苷两亲物(XMA)

Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation.

作者信息

Cho Kyung Ho, Du Yang, Scull Nicola J, Hariharan Parameswaran, Gotfryd Kamil, Loland Claus J, Guan Lan, Byrne Bernadette, Kobilka Brian K, Chae Pil Seok

机构信息

Department of Bionanotechnology, Hanyang University, Ansan, 426-791 (Republic of Korea).

Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305 (USA).

出版信息

Chemistry. 2015 Jul 6;21(28):10008-13. doi: 10.1002/chem.201501083. Epub 2015 May 26.

Abstract

Membrane proteins are key functional players in biological systems. These biomacromolecules contain both hydrophilic and hydrophobic regions and thus amphipathic molecules are necessary to extract membrane proteins from their native lipid environments and stabilise them in aqueous solutions. Conventional detergents are commonly used for membrane protein manipulation, but membrane proteins surrounded by these agents often undergo denaturation and aggregation. In this study, a novel class of maltoside-bearing amphiphiles, with a xylene linker in the central region, designated xylene-linked maltoside amphiphiles (XMAs) was developed. When these novel agents were evaluated with a number of membrane proteins, it was found that XMA-4 and XMA-5 have particularly favourable efficacy with respect to membrane protein stabilisation, indicating that these agents hold significant potential for membrane protein structural study.

摘要

膜蛋白是生物系统中的关键功能分子。这些生物大分子同时包含亲水区域和疏水区域,因此两亲性分子对于从其天然脂质环境中提取膜蛋白并使其在水溶液中稳定是必不可少的。传统洗涤剂常用于膜蛋白操作,但被这些试剂包围的膜蛋白常常会发生变性和聚集。在本研究中,开发了一类新型的带有麦芽糖苷的两亲物,其中心区域含有二甲苯连接基,命名为二甲苯连接的麦芽糖苷两亲物(XMA)。当用多种膜蛋白对这些新型试剂进行评估时,发现XMA-4和XMA-5在膜蛋白稳定方面具有特别良好的效果,这表明这些试剂在膜蛋白结构研究方面具有巨大潜力。

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