Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies
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Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies. / Ehsan, Muhammad; Du, Yang; Scull, Nicola J; Tikhonova, Elena; Tarrasch, Jeffrey; Mortensen, Jonas S; Loland, Claus J; Skiniotis, Georgios; Guan, Lan; Byrne, Bernadette; Kobilka, Brian K; Chae, Pil Seok.
In: Journal of the American Chemical Society, Vol. 138, No. 11, 23.03.2016, p. 3789-3796.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies
AU - Ehsan, Muhammad
AU - Du, Yang
AU - Scull, Nicola J
AU - Tikhonova, Elena
AU - Tarrasch, Jeffrey
AU - Mortensen, Jonas S
AU - Loland, Claus J
AU - Skiniotis, Georgios
AU - Guan, Lan
AU - Byrne, Bernadette
AU - Kobilka, Brian K
AU - Chae, Pil Seok
PY - 2016/3/23
Y1 - 2016/3/23
N2 - Detergents are essential tools for membrane protein manipulation. Micelles formed by detergent molecules have the ability to encapsulate the hydrophobic domains of membrane proteins. The resulting protein-detergent complexes (PDCs) are compatible with the polar environments of aqueous media, making structural and functional analysis feasible. Although a number of novel agents have been developed to overcome the limitations of conventional detergents, most have traditional head groups such as glucoside or maltoside. In this study, we introduce a class of amphiphiles, the PSA/Es with a novel highly branched pentasaccharide hydrophilic group. The PSA/Es conferred markedly increased stability to a diverse range of membrane proteins compared to conventional detergents, indicating a positive role for the new hydrophilic group in maintaining the native protein integrity. In addition, PDCs formed by PSA/Es were smaller and more suitable for electron microscopic analysis than those formed by DDM, indicating that the new agents have significant potential for the structure-function studies of membrane proteins.
AB - Detergents are essential tools for membrane protein manipulation. Micelles formed by detergent molecules have the ability to encapsulate the hydrophobic domains of membrane proteins. The resulting protein-detergent complexes (PDCs) are compatible with the polar environments of aqueous media, making structural and functional analysis feasible. Although a number of novel agents have been developed to overcome the limitations of conventional detergents, most have traditional head groups such as glucoside or maltoside. In this study, we introduce a class of amphiphiles, the PSA/Es with a novel highly branched pentasaccharide hydrophilic group. The PSA/Es conferred markedly increased stability to a diverse range of membrane proteins compared to conventional detergents, indicating a positive role for the new hydrophilic group in maintaining the native protein integrity. In addition, PDCs formed by PSA/Es were smaller and more suitable for electron microscopic analysis than those formed by DDM, indicating that the new agents have significant potential for the structure-function studies of membrane proteins.
U2 - 10.1021/jacs.5b13233
DO - 10.1021/jacs.5b13233
M3 - Journal article
C2 - 26966956
VL - 138
SP - 3789
EP - 3796
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 11
ER -
ID: 167932728