Imperial College London

ProfessorBernadetteByrne

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology
 
 
 
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Contact

 

+44 (0)20 7594 3004b.byrne Website

 
 
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Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Das:2019:10.1039/c8ob03153c,
author = {Das, M and Du, Y and Mortensen, JS and Ramos, M and Ghani, L and Lee, HJ and Bae, HE and Byrne, B and Guan, L and Loland, CJ and Kobilka, BK and Chae, PS},
doi = {10.1039/c8ob03153c},
journal = {Organic and Biomolecular Chemistry},
pages = {3249--3257},
title = {Trehalose-cored amphiphiles for membrane protein stabilization: importance of the detergent micelle size in GPCR stability},
url = {http://dx.doi.org/10.1039/c8ob03153c},
volume = {17},
year = {2019}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Despite their importance in biology and medicinal chemistry, structural and functional studies of membrane proteins present major challenges. To study diverse membrane proteins, it is crucial to have the correct detergent to efficiently extract and stabilize the proteins from the native membranes for biochemical/biophysical downstream analyses. But many membrane proteins, particularly eukaryotic ones, are recalcitrant to stabilization and/or crystallization with currently available detergents and thus there are major efforts to develop novel detergents with enhanced properties. Here, a novel class of trehalose-cored amphiphiles are introduced, with multiple alkyl chains and carbohydrates projecting from the trehalose core unit are introduced. A few members displayed enhanced protein stabilization behavior compared to the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for multiple tested membrane proteins: (i) a bacterial leucine transporter (LeuT), (ii) the R. capsulatus photosynthetic superassembly, and (iii) the human β2 adrenergic receptor (β2AR). Due to synthetic convenience and their favourable behaviors for a range of membrane proteins, these agents have potential for membrane protein research. In addition, the detergent property-efficacy relationship discussed here will guide future design of novel detergents.
AU - Das,M
AU - Du,Y
AU - Mortensen,JS
AU - Ramos,M
AU - Ghani,L
AU - Lee,HJ
AU - Bae,HE
AU - Byrne,B
AU - Guan,L
AU - Loland,CJ
AU - Kobilka,BK
AU - Chae,PS
DO - 10.1039/c8ob03153c
EP - 3257
PY - 2019///
SN - 1477-0520
SP - 3249
TI - Trehalose-cored amphiphiles for membrane protein stabilization: importance of the detergent micelle size in GPCR stability
T2 - Organic and Biomolecular Chemistry
UR - http://dx.doi.org/10.1039/c8ob03153c
UR - https://www.ncbi.nlm.nih.gov/pubmed/30843907
UR - http://hdl.handle.net/10044/1/76823
VL - 17
ER -