A class of rigid linker-bearing glucosides for membrane protein structural study
- Authors
- Sadaf, Aiman; Mortensen, Jonas S.; Capaldi, Stefano; Tikhonova, Elena; Hariharan, Parameswaran; Ribeiro, Orquidea; Loland, Claus J.; Guan, Lan; Byrne, Bernadette; Chae, Pil Seok
- Issue Date
- Mar-2016
- Publisher
- Royal Society of Chemistry
- Citation
- Chemical Science, v.7, no.3, pp.1933 - 1939
- Indexed
- SCIE
SCOPUS
- Journal Title
- Chemical Science
- Volume
- 7
- Number
- 3
- Start Page
- 1933
- End Page
- 1939
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/16050
- DOI
- 10.1039/c5sc02900g
- ISSN
- 2041-6520
- 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.
- Files in This Item
-
Go to Link
- Appears in
Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/16050)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.