Bae Hyoung Eun, Du Yang, Hariharan Parameswaran, Mortensen Jonas S, Kumar Kaavya K, Ha Betty, Das Manabendra, Lee Hyun Sung, Loland Claus J, Guan Lan, Kobilka Brian K, Chae Pil Seok
Department of Bionanotechnology , Hanyang University , Ansan , 15588 Korea . Email:
Molecular and Cellular Physiology , Stanford , CA 94305 , USA . Email:
Chem Sci. 2018 Nov 5;10(4):1107-1116. doi: 10.1039/c8sc02560f. eCollection 2019 Jan 28.
Maintaining protein stability in an aqueous solution is a prerequisite for protein structural and functional studies, but conventional detergents have increasingly showed limited ability to maintain protein integrity. A representative novel agent, maltose neopentyl glycol-3 (MNG-3), has recently substantially contributed to membrane protein structural studies. Motivated by the popular use of this novel agent, we prepared asymmetric versions of MNG-3 and evaluated these agents with several membrane proteins including two G protein-coupled receptors in this study. We found that some new MNGs were significantly more effective than MNG-3 at preserving protein integrity in the long term, suggesting that these asymmetric MNGs will find a wide use in membrane protein studies. In addition, this is the first study addressing the favorable effect of detergent asymmetric nature on membrane protein stability.
在水溶液中维持蛋白质稳定性是蛋白质结构和功能研究的前提条件，但传统去污剂维持蛋白质完整性的能力越来越有限。一种具有代表性的新型试剂，麦芽糖醇新戊二醇-3（MNG-3），最近在膜蛋白结构研究中做出了重大贡献。受这种新型试剂广泛应用的启发，我们制备了MNG-3的不对称变体，并在本研究中用几种膜蛋白（包括两种G蛋白偶联受体）对这些试剂进行了评估。我们发现，一些新型MNG在长期保持蛋白质完整性方面比MNG-3显著更有效，这表明这些不对称MNG将在膜蛋白研究中得到广泛应用。此外，这是第一项探讨去污剂不对称性质对膜蛋白稳定性有利影响的研究。
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