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Novel Tripod Amphiphiles for Membrane Protein Analysis
Author(s) -
Chae Pil Seok,
Kruse Andrew C.,
Gotfryd Kamil,
Rana Rohini R.,
Cho Kyung Ho,
Rasmussen Søren G. F.,
Bae Hyoung Eun,
Chandra Richa,
Gether Ulrik,
Guan Lan,
Kobilka Brian K.,
Loland Claus J.,
Byrne Bernadette,
Gellman Samuel H.
Publication year - 2013
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.201301423
Subject(s) - tripod (photography) , amphiphile , membrane , membrane protein , chemistry , amphiphilic molecule , biophysics , biochemistry , biology , organic chemistry , engineering , copolymer , mechanical engineering , polymer
Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.