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Novel Xylene‐Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation
Author(s) -
Cho Kyung Ho,
Du Yang,
Scull Nicola J.,
Hariharan Parameswaran,
Gotfryd Kamil,
Loland Claus J.,
Guan Lan,
Byrne Bernadette,
Kobilka Brian K.,
Chae Pil Seok
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201501083
Subject(s) - amphiphile , membrane , chemistry , membrane protein , protein–lipid interaction , aqueous solution , peripheral membrane protein , liposome , lipid bilayer , denaturation (fissile materials) , integral membrane protein , biophysics , biochemistry , organic chemistry , biology , polymer , nuclear chemistry , copolymer
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.