Imperial College London
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ProfessorBernadetteByrne

Faculty of Natural Sciences, Department of Life Sciences

Associate Dean (Equality, Diversity and Inclusion) for FoNS
 
 
 
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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:2020:10.1021/jacs.0c09629,
author = {Das, M and Mahler, F and Hariharan, P and Wang, H and Du, Y and Mortensen, JS and Patallo, EP and Ghani, L and Glueck, D and Lee, HJ and Byrne, B and Loland, CJ and Guan, L and Kobilka, BK and Keller, S and Chae, PS},
doi = {10.1021/jacs.0c09629},
journal = {Journal of the American Chemical Society},
pages = {21382--21392},
title = {Diastereomeric Cyclopentane-Based Maltosides (CPMs) as tools for membrane protein study},
url = {http://dx.doi.org/10.1021/jacs.0c09629},
volume = {142},
year = {2020}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Amphiphilic agents, called detergents, are invaluable tools for studying membrane proteins. However, membrane proteins encapsulated by conventional head-to-tail detergents tend to denature or aggregate, necessitating the development of structurally distinct molecules with improved efficacy. Here, a novel class of diastereomeric detergents with a cyclopentane core unit, designated cyclopentane-based maltosides (CPMs), were prepared and evaluated for their ability to solubilize and stabilize several model membrane proteins. A couple of CPMs displayed enhanced behavior compared with the benchmark conventional detergent, n-dodecyl-β-d-maltoside (DDM), for all the tested membrane proteins including two G-protein-coupled receptors (GPCRs). Furthermore, CPM-C12 was notable for its ability to confer enhanced membrane protein stability compared with the previously developed conformationally rigid NBMs [J. Am. Chem. Soc.2017, 139, 3072] and LMNG. The effect of the individual CPMs on protein stability varied depending on both the detergent configuration (cis/trans) and alkyl chain length, allowing us draw conclusions on the detergent structure–property–efficacy relationship. Thus, this study not only provides novel detergent tools useful for membrane protein research but also reports on structural features of the detergents critical for detergent efficacy in stabilizing membrane proteins.
AU  - Das,M
AU  - Mahler,F
AU  - Hariharan,P
AU  - Wang,H
AU  - Du,Y
AU  - Mortensen,JS
AU  - Patallo,EP
AU  - Ghani,L
AU  - Glueck,D
AU  - Lee,HJ
AU  - Byrne,B
AU  - Loland,CJ
AU  - Guan,L
AU  - Kobilka,BK
AU  - Keller,S
AU  - Chae,PS
DO  - 10.1021/jacs.0c09629
EP  - 21392
PY  - 2020///
SN  - 0002-7863
SP  - 21382
TI  - Diastereomeric Cyclopentane-Based Maltosides (CPMs) as tools for membrane protein study
T2  - Journal of the American Chemical Society
UR  - http://dx.doi.org/10.1021/jacs.0c09629
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000603395100019&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://pubs.acs.org/doi/10.1021/jacs.0c09629
UR  - http://hdl.handle.net/10044/1/89890
VL  - 142
ER  -
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