Issue 3, 2016

A class of rigid linker-bearing glucosides for membrane protein structural study

Abstract

Membrane proteins are amphipathic bio-macromolecules incompatible with the polar environments of aqueous media. Conventional detergents encapsulate the hydrophobic surfaces of membrane proteins allowing them to exist in aqueous solution. Membrane proteins stabilized by detergent micelles are used for structural and functional analysis. Despite the availability of a large number of detergents, only a few agents are sufficiently effective at maintaining the integrity of membrane proteins to allow successful crystallization. In the present study, we describe a novel class of synthetic amphiphiles with a branched tail group and a triglucoside head group. These head and tail groups were connected via an amide or ether linkage by using a tris(hydroxylmethyl)aminomethane (TRIS) or neopentyl glycol (NPG) linker to produce TRIS-derived triglucosides (TDTs) and NPG-derived triglucosides (NDTs), respectively. Members of this class conferred enhanced stability on target membrane proteins compared to conventional detergents. Because of straightforward synthesis of the novel agents and their favourable effects on a range of membrane proteins, these agents should be of wide applicability to membrane protein science.

Graphical abstract: A class of rigid linker-bearing glucosides for membrane protein structural study

Supplementary files

Article information

Article type
Edge Article
Submitted
06 Aug 2015
Accepted
29 Nov 2015
First published
16 Dec 2015
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2016,7, 1933-1939

Author version available

A class of rigid linker-bearing glucosides for membrane protein structural study

A. Sadaf, J. S. Mortensen, S. Capaldi, E. Tikhonova, P. Hariharan, O. Ribeiro, C. J. Loland, L. Guan, B. Byrne and P. S. Chae, Chem. Sci., 2016, 7, 1933 DOI: 10.1039/C5SC02900G

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