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. / Sadaf, Aiman; Mortensen, Jonas S; Capaldi, Stefano; Tikhonova, Elena; Hariharan, Parameswaran; de Castro Ribeiro, Orquidea; Loland, Claus J; Guan, Lan; Byrne, Bernadette; Chae, Pil Seok.
In: Chemical Science, Vol. 7, No. 3, 01.03.2016, p. 1933-1939.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - A Class of Rigid Linker-bearing Glucosides for Membrane Protein Structural Study
AU - Sadaf, Aiman
AU - Mortensen, Jonas S
AU - Capaldi, Stefano
AU - Tikhonova, Elena
AU - Hariharan, Parameswaran
AU - de Castro Ribeiro, Orquidea
AU - Loland, Claus J
AU - Guan, Lan
AU - Byrne, Bernadette
AU - Chae, Pil Seok
PY - 2016/3/1
Y1 - 2016/3/1
N2 - 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.
AB - 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.
U2 - 10.1039/C5SC02900G
DO - 10.1039/C5SC02900G
M3 - Journal article
C2 - 27110345
VL - 7
SP - 1933
EP - 1939
JO - Chemical Science
JF - Chemical Science
SN - 2041-6520
IS - 3
ER -
ID: 167932663