title: Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation.
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.
authors.affiliation: Department of Bionanotechnology, Hanyang University, Ansan, 426-791 (Republic of Korea).
authors.forename: Kyung Ho
authors.initials: KH
authors.lastname: Cho
authors.affiliation: Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305 (USA).
authors.forename: Yang
authors.initials: Y
authors.lastname: Du
authors.affiliation: Department of Life Sciences, Imperial College London, London, SW7 2AZ (UK).
authors.forename: Nicola J
authors.initials: NJ
authors.lastname: Scull
authors.affiliation: Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430 (USA).
authors.forename: Parameswaran
authors.initials: P
authors.lastname: Hariharan
authors.affiliation: Department of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen (Denmark).|Present address: Department of Biomedical Sciences, University of Copenhagen, 2200 Copenhagen (Denmark).
authors.forename: Kamil
authors.initials: K
authors.lastname: Gotfryd
authors.affiliation: Department of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen (Denmark).
authors.forename: Claus J
authors.initials: CJ
authors.lastname: Loland
authors.affiliation: Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX 79430 (USA).
authors.forename: Lan
authors.initials: L
authors.lastname: Guan
authors.affiliation: Department of Life Sciences, Imperial College London, London, SW7 2AZ (UK).
authors.forename: Bernadette
authors.initials: B
authors.lastname: Byrne
authors.affiliation: Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305 (USA).
authors.forename: Brian K
authors.initials: BK
authors.lastname: Kobilka
authors.affiliation: Department of Bionanotechnology, Hanyang University, Ansan, 426-791 (Republic of Korea). pchae@hanyang.ac.kr.
authors.forename: Pil Seok
authors.initials: PS
authors.lastname: Chae
mesh_terms: D003902:Detergents / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D046911:Macromolecular Substances / Q000737:chemistry*; D008320:Maltose / Q000031:analogs & derivatives* / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D012995:Solubility; D013501:Surface-Active Agents; D014992:Xylenes / Q000737:chemistry*
chemical_list: D003902:Detergents; D046911:Macromolecular Substances; D008565:Membrane Proteins; D013501:Surface-Active Agents; D014992:Xylenes; D008320:Maltose
keywords: amphiphile design; detergents; membrane proteins; protein stabilisation; protein structure