Department of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea.
Molecular and Cellular Physiology, Stanford, CA, 94305, USA.
Chemistry. 2018 Jul 11;24(39):9860-9868. doi: 10.1002/chem.201801141. Epub 2018 Jun 13.
Amphiphiles are critical tools for the structural and functional study of membrane proteins. Membrane proteins encapsulated by conventional head-to-tail detergents tend to undergo structural degradation, necessitating the development of structurally novel agents with improved efficacy. In recent years, facial amphiphiles have yielded encouraging results in terms of membrane protein stability. Herein, we report a new facial detergent (i.e., LFA-C4) that confers greater stability to tested membrane proteins than the bola form analogue. Owing to the increased facial property and the adaptability of the detergent micelles in complex with different membrane proteins, LFA-C4 yields increased stability compared to n-dodecyl-β-d-maltoside (DDM). Thus, this study not only describes a novel maltoside detergent with enhanced protein-stabilizing properties, but also shows that the customizable nature of a detergent plays an important role in the stabilization of membrane proteins. Owing to both synthetic convenience and enhanced stabilization efficacy for a range of membrane proteins, the new agent has major potential in membrane protein research.
两亲分子是研究膜蛋白结构和功能的重要工具。用传统的头对头去污剂包裹的膜蛋白往往会发生结构降解，因此需要开发具有更好效果的结构新颖的试剂。近年来，在膜蛋白稳定性方面，两亲分子取得了令人鼓舞的结果。本文报道了一种新的两亲分子清洁剂（即 LFA-C4），与类似的棒状形式相比，它能赋予更多测试膜蛋白稳定性。由于增加了两亲性和与不同膜蛋白形成的胶束的适应性，LFA-C4 比正十二烷基-β-D-麦芽糖苷（DDM）具有更高的稳定性。因此，本研究不仅描述了一种具有增强蛋白稳定特性的新型麦芽糖苷清洁剂，还表明清洁剂的可定制性质在膜蛋白的稳定中起着重要作用。由于其合成方便性和对多种膜蛋白的增强稳定效果，这种新试剂在膜蛋白研究中具有重要的应用潜力。
