Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins

被引：186

作者：

Chae, Pil Seok ^{[1
]}

Rasmussen, Soren G. F. ^{[2
]}

Rana, Rohini R. ^{[3
]}

Gotfryd, Kamil ^{[4
]}

Chandra, Richa ^{[5
]}

Goren, Michael A. ^{[6
]}

Kruse, Andrew C. ^{[2
]}

Nurva, Shailika ^{[5
]}

Loland, Claus J. ^{[4
]}

Pierre, Yves ^{[7
]}

Drew, David ^{[3
]}

Popot, Jean-Luc ^{[7
]}

Picot, Daniel ^{[7
]}

Fox, Brian G. ^{[6
,8
]}

Guan, Lan ^{[5
]}

Gether, Ulrik ^{[4
]}

Byrne, Bernadette ^{[3
]}

Kobilka, Brian ^{[2
]}

Gellman, Samuel H. ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Stanford Univ, Stanford, CA 94305 USA

[3] Univ London Imperial Coll Sci Technol & Med, Dept Life Sci, Div Mol Biosci, London, England

[4] Univ Copenhagen, Fac Hlth Sci, Mol Neuropharmacol Grp, Dept Neurosci & Pharmacol, Copenhagen, Denmark

[5] Texas Tech Univ, Hlth Sci Ctr, Ctr Membrane Prot Res, Dept Cell Physiol & Mol Biophys, Lubbock, TX 79430 USA

[6] Univ Wisconsin, Dept Biochem, Madison, WI 53705 USA

[7] Univ Paris 07, CNRS, Lab Biol Physicochim Prot Membranaires, Inst Biol Physicochim,UMR 7099, Paris, France

[8] Univ Wisconsin, Ctr Eukaryot Struct Genom, Madison, WI USA

来源：

NATURE METHODS | 2010年 / 7卷 / 12期

基金：

美国国家卫生研究院;

关键词：

MELIBIOSE PERMEASE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; PURIFICATION; SURFACTANTS; OVEREXPRESSION; OPTIMIZATION; DETERGENTS; NANODISCS; AMPHIPOLS;

D O I：

10.1038/NMETH.1526

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.

引用

页码：1003 / U90

页数：9

共 43 条

[1] PHENIX:: building new software for automated crystallographic structure determination [J].