Solubilization of Membrane Proteins into Functional Lipid-Bilayer Nanodiscs Using a Diisobutylene/Maleic Acid Copolymer

被引：209

作者：

Oluwole, Abraham Olusegun ^{[1
,2
]}

Danielczak, Bartholomaeus ^{[1
]}

Meister, Annette ^{[3
,4
]}

Babalola, Jonathan Oyebamiji ^{[2
]}

Vargas, Carolyn ^{[1
]}

Keller, Sandro ^{[1
]}

机构：

[1] Univ Kaiserslautern, Mol Biophys, Erwin Schrodinger Str 13, D-67663 Kaiserslautern, Germany

[2] Univ Ibadan, Dept Chem, Ibadan 200284, Nigeria

[3] Martin Luther Univ Halle Wittenberg, Inst Chem, Von Danckelmann Pl 4, D-06120 Halle, Germany

[4] Martin Luther Univ Halle Wittenberg, Inst Biochem & Biotechnol, Von Danckelmann Pl 4, D-06120 Halle, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2017年 / 56卷 / 07期

关键词：

amphiphilic polymers; biomembranes; membrane proteins; membrane mimetics; protein chromatography; DETERGENT-FREE ISOLATION; PHOSPHOLIPASE-A; SPECTROSCOPY; PARTICLES; LIPODISQ;

D O I：

10.1002/anie.201610778

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Once removed from their natural environment, membrane proteins depend on membrane-mimetic systems to retain their native structures and functions. To this end, lipid-bilayer nanodiscs that are bounded by scaffold proteins or amphiphilic polymers such as styrene/maleic acid (SMA) copolymers have been introduced as alternatives to detergent micelles and liposomes for in vitro membrane-protein research. Herein, we show that an alternating diisobutylene/maleic acid (DIBMA) copolymer shows equal performance to SMA in solubilizing phospholipids, stabilizes an integral membrane enzyme in functional bilayer nanodiscs, and extracts proteins of various sizes directly from cellular membranes. Unlike aromatic SMA, aliphatic DIBMA has only a mild effect on lipid acyl-chain order, does not interfere with optical spectroscopy in the far-UV range, and does not precipitate in the presence of low millimolar concentrations of divalent cations.

引用

页码：1919 / 1924

页数：6

共 30 条

[1] Detergent selection for enhanced extraction of membrane proteins [J].