Premium
New tensio‐active molecules stabilize a human G protein‐coupled receptor in solution
Author(s) -
Damian Marjorie,
Perino Sandrine,
Polidori Ange,
Martin Aimée,
Serre Laurence,
Pucci Bernard,
Banères Jean-Louis
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.091
Subject(s) - chemistry , reagent , hydroxymethyl , phospholipid , tris , molecule , membrane , membrane protein , stereochemistry , biochemistry , organic chemistry
Structural characterization of membrane proteins is hampered by the instability of the isolated proteins in detergent solutions. Here, we describe a new class of phospholipid‐like surfactants that stabilize the G protein‐coupled receptor, BLT1. These compounds, called C 13 U 9 , C 13 U 19 , C 15 U 25 and C 17 U 16 , were synthesized by radical polymerization of Tris(hydroxymethyl) acrylamidomethane in the presence of thioglycerol, first endowed with two hydrocarbon chains with variable lengths (13–17 carbon atoms), as transfer reagent. C 13 U 19 , C 17 U 16 or C 15 U 25 significantly enhanced the stability of BLT1 in solution compared to what was obtained with common detergents. These molecules therefore represent a promising step towards the structural characterization of BLT1 and possibly other membrane proteins.