2. Academic Validation
  3. New Malonate-Derived Tetraglucoside Detergents for Membrane Protein Stability

New Malonate-Derived Tetraglucoside Detergents for Membrane Protein Stability

  • ACS Chem Biol. 2020 Jun 19;15(6):1697-1707. doi: 10.1021/acschembio.0c00316.
Muhammad Ehsan 1,  Satoshi Katsube 2,  Cristina Cecchetti 3,  Yang Du 4,  Jonas S Mortensen 5,  Haoqing Wang 6,  Andreas Nygaard 5,  Lubna Ghani 1,  Claus J Loland 5,  Brian K Kobilka 6,  Bernadette Byrne 3,  Lan Guan 2,  Pil Seok Chae 1
Affiliations

Affiliations

  • 1 Department of Bionanotechnology, Hanyang University, Ansan, 15588, Korea.
  • 2 Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, United States.
  • 3 Department of Life Sciences, Imperial College London, London, SW7 2AZ, United Kingdom.
  • 4 School of Life and Health Sciences, Kobilka Institute of Innovative Drug Discovery, Chinese University of Hong Kong, 2001 Longxiang Avenue, Shenzhen, Guangdong 518172, China.
  • 5 Department of Neuroscience, University of Copenhagen, Copenhagen, DK-2200, Denmark.
  • 6 Molecular and Cellular Physiology, Stanford University, Stanford, California 94305, United States.
PMID: 32501004 DOI: 10.1021/acschembio.0c00316
Abstract

Membrane proteins are widely studied in detergent micelles, a membrane-mimetic system formed by amphiphilic compounds. However, classical detergents have serious limitations in their utility, particularly for unstable proteins such as eukaryotic membrane proteins and membrane protein complexes, and thus, there is an unmet need for novel amphiphiles with enhanced ability to stabilize membrane proteins. Here, we developed a new class of malonate-derived detergents with four glucosides, designated malonate-derived tetra-glucosides (MTGs), and compared these new detergents with previously reported octyl glucose neopentyl glycol (OGNG) and n-dodecyl-β-d-maltoside (DDM). When tested with two G-protein coupled receptors (GPCRs) and three transporters, a couple of MTGs consistently conferred enhanced stability to all tested proteins compared to DDM and OGNG. As a result of favorable behaviors for a range of membrane proteins, these MTGs have substantial potential for membrane protein research. This study additionally provides a new detergent design principle based on the effect of a polar functional group (i.e., ether) on protein stability depending on its position in the detergent scaffold.

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