NDLI: Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Byrne, Bernadette Scull, Nicola J. Hussain, Hazrat Tarrasch, Jeffrey Kobilka, Brian K. Chae, Pil Seok Mortensen, Jonas S. Loland, Claus J. Du, Yang Bae, Hyoung Eun
Description	Author Affiliation: Hussain H ( Department of Bionanotechnology, Hanyang University, Ansan, 426-791, Korea.); Du Y ( Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.); Scull NJ ( Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK.); Mortensen JS ( Department of Neuroscience and Pharmacology, University of Copenhagen, Copenhagen, DK-2200, Denmark.); Tarrasch J ( Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.); Bae HE ( Department of Bionanotechnology, Hanyang University, Ansan, 426-791, Korea.); Loland CJ ( Department of Neuroscience and Pharmacology, University of Copenhagen, Copenhagen, DK-2200, Denmark.); Byrne B ( Department of Life Sciences, Imperial College London, London, SW7 2AZ, UK.); Kobilka BK ( Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.); Chae PS ( Department of Bionanotechnology, Hanyang University, Ansan, 426-791, Korea. pchae@hanyang.ac.kr.)
Abstract	Integral membrane proteins are amphipathic molecules crucial for all cellular life. The structural study of these macromolecules starts with protein extraction from the native membranes, followed by purification and crystallisation. Detergents are essential tools for these processes, but detergent-solubilised membrane proteins often denature and aggregate, resulting in loss of both structure and function. In this study, a novel class of agents, designated mannitol-based amphiphiles (MNAs), were prepared and characterised for their ability to solubilise and stabilise membrane proteins. Some of MNAs conferred enhanced stability to four membrane proteins including a G protein-coupled receptor (GPCR), the $β_{2}$ adrenergic receptor $(β_{2}AR),$ compared to both n-dodecyl-d-maltoside (DDM) and the other MNAs. These agents were also better than DDM for electron microscopy analysis of the $β_{2}AR.$ The ease of preparation together with the enhanced membrane protein stabilisation efficacy demonstrates the value of these agents for future membrane protein research.
ISSN	09476539
e-ISSN	15213765
Journal	Chemistry - A European Journal
Issue Number	21
Volume Number	22
Language	English
Publisher	Wiley-VCH;ChemPubSoc Europe
Publisher Date	2016-05-17
Publisher Place	Germany
Access Restriction	Open
Subject Keyword	Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Catalysis

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