New tensio-active molecules stabilize a human G protein-coupled receptor in solution

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 13U 9, C 13U 19, C 15U 25 and...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2007-05, Vol.581 (10), p.1944-1950
Main Authors: Damian, Marjorie, Perino, Sandrine, Polidori, Ange, Martin, Aimée, Serre, Laurence, Pucci, Bernard, Banères, Jean-Louis
Format: Article
Language:English
Subjects:
Acrylamides
Acrylamides - chemistry
AIBN
circular dichroism
cmc
critical micellar concentration
DDM
degree of polymerization
Detergent
Dimerization
dodecyl-β-d-maltoside
dodecyldimethylamino oxide
DP n
G protein-coupled receptors
GPCR
GPCRs
HDM
hexadecyl-β-d-maltoside
Humans
LDAO
Leukotriene B4
Leukotriene B4 - metabolism
Life Sciences
Ligands
LTB4
Membrane protein
Neurons and Cognition
Protein Folding
Receptors, Leukotriene B4
Receptors, Leukotriene B4 - chemistry
Receptors, Leukotriene B4 - metabolism
Solutions
Solutions - chemistry
Surface-Active Agents
Surface-Active Agents - chemistry
Surfactant
TEA
tetrahydrofuran
THAM
Thermodynamics
THF
Time Factors
triethylamine
Tris(hydroxymethyl)acrylamidomethane
α,α′-azobis isobutyronitrile
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 13U 9, C 13U 19, C 15U 25 and C 17U 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 13U 19, C 17U 16 or C 15U 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.03.091