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

被引：9

作者：

Damian, Marjorie

Perino, Sandrine

Polidori, Ange

Martin, Aimee

Serre, Laurence

Pucci, Bernard

Baneres, Jean-Louis

机构：

[1] Univ Montpellier I, CNRS, UMR 5247, Inst Biomol Max Mousseron,Fac Pharm, F-34093 Montpellier 5, France

[2] Univ Montpellier 2, CNRS, UMR 5247, Inst Biomol Max Mousseron,Fac Pharm, F-34093 Montpellier 5, France

[3] Univ Avignon & Pays Vaucluse, Fac Sci, Lab Chim Bioorgan & Syst Mol Vectoriels, F-84000 Avignon, France

[4] UJF, CNRS, CEA, Lab Prot Membranaires,Inst Biol Struct Jean Pierr, F-38027 Grenoble 01, France

来源：

FEBS LETTERS | 2007年 / 581卷 / 10期

关键词：

GPCR; membrane protein; surfactant; detergent;

D O I：

10.1016/j.febslet.2007.03.091

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 C13U9, C13U9, C15U25 and C17U16, were synthesized by radical polymerization of Tris(hydroxymethyl) acrylamidomethane in the presence of thioglycerol, first endowed with two hydrocarbon chains with variable lengths (1317 carbon atoms), as transfer reagent. C13U19,, C17U16 or C15U25 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 BLTI and possibly other membrane proteins. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1944 / 1950

页数：7

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