NDLI: A Class of Rigid Linker-bearing Glucosides for Membrane Protein Structural Study

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A Class of Rigid Linker-bearing Glucosides for Membrane Protein Structural Study

Content Provider	PubMed Central
Author	Sadaf, Aiman Mortensen, Jonas S. Capaldi, Stefano Tikhonova, Elena Hariharan, Parameswaran Ribeiro, Orquidea De Castro Loland, Claus J. Guan, Lan Byrne, Bernadette Chae, Pil Seok
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.
Related Links	http://dx.doi.org/10.1039/C5SC02900G
Ending Page	1939
Page Count	7
Starting Page	1933
File Format	PDF
ISSN	20416539
e-ISSN	20416539
Journal	Chemical science (Royal Society of Chemistry : 2010)
Issue Number	3
Volume Number	7
Language	English
Publisher Date	2016-03-01
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Chemistry

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