Highly branched pentasaccharide-bearing amphiphiles for membrane protein studies
File(s)
Accepted version
Author(s)
Type
Journal Article
Abstract
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.
Date Issued
2016-03-23
Date Acceptance
2016-03-11
Citation
Journal of the American Chemical Society, 2016, 138 (11), pp.3789-3796
ISSN
1520-5126
Publisher
American Chemical Society
Start Page
3789
End Page
3796
Journal / Book Title
Journal of the American Chemical Society
Volume
138
Issue
11
Copyright Statement
This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of the American Chemical Society, © 2016 American Chemical Society, after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/jacs.5b13233
Sponsor
Biotechnology and Biological Sciences Research Council (BBSRC)
Identifier
https://pubs.acs.org/doi/10.1021/jacs.5b13233
Grant Number
BB/K017292/1
Subjects
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
CRYSTAL-STRUCTURE
FACIAL AMPHIPHILES
BETA(2)-ADRENERGIC RECEPTOR
STRUCTURAL INSIGHTS
STABILIZATION
CRYSTALLIZATION
DETERGENTS
SOLUBILIZATION
COMPLEX
FLUORESCENCE
Antiporters
Arabidopsis Proteins
Carbohydrate Sequence
Detergents
Green Fluorescent Proteins
Hydrophobic and Hydrophilic Interactions
Membrane Proteins
Micelles
Models, Molecular
Oligosaccharides, Branched-Chain
Recombinant Fusion Proteins
Spectrometry, Fluorescence
Structure-Activity Relationship
Oligosaccharides, Branched-Chain
Antiporters
Green Fluorescent Proteins
Membrane Proteins
Arabidopsis Proteins
Recombinant Fusion Proteins
Detergents
Spectrometry, Fluorescence
Carbohydrate Sequence
Structure-Activity Relationship
Micelles
Models, Molecular
Hydrophobic and Hydrophilic Interactions
03 Chemical Sciences
General Chemistry
Publication Status
Published
Date Publish Online
2016-03-11