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{Ehsan:2019:10.1002/chem.201902468,
author = {Ehsan, M and Du, Y and Mortensen, JS and Hariharan, P and Qu, Q and Ghani, L and Das, M and Grethen, A and Byrne, B and Skiniotis, G and Keller, S and Loland, CJ and Guan, L and Kobilka, BK and Chae, PS},
doi = {10.1002/chem.201902468},
journal = {Chemistry - A European Journal},
pages = {11545--11554},
title = {Self-assembly behavior and application of terphenyl-cored trimaltosides for membrane-protein studies: impact of detergent hydrophobic group geometry on protein stability},
url = {http://dx.doi.org/10.1002/chem.201902468},
volume = {25},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Amphipathic agents are widely used in various fields including biomedical sciences. Micelle-forming detergents are particularly useful for in vitro membrane-protein characterization. As many conventional detergents are limited in their ability to stabilize membrane proteins, it is necessary to develop novel detergents to facilitate membrane-protein research. In the current study, we developed novel trimaltoside detergents with an alkyl pendant-bearing terphenyl unit as a hydrophobic group, designated terphenyl-cored maltosides (TPMs). We found that the geometry of the detergent hydrophobic group substantially impacts detergent self-assembly behavior, as well as detergent efficacy for membrane-protein stabilization. TPM-Vs, with a bent terphenyl group, were superior to the linear counterparts (TPM-Ls) at stabilizing multiple membrane proteins. The favorable protein stabilization efficacy of these bent TPMs is likely associated with a binding mode with membrane proteins distinct from conventional detergents and facial amphiphiles. When compared to n-dodecyl-β-d-maltoside (DDM), most TPMs were superior or comparable to this gold standard detergent at stabilizing membrane proteins. Notably, TPM-L3 was particularly effective at stabilizing the human β2 adrenergic receptor (β2 AR), a G-protein coupled receptor, and its complex with Gs protein. Thus, the current study not only provides novel detergent tools that are useful for membrane-protein study, but also suggests a critical role for detergent hydrophobic group geometry in governing detergent efficacy.
AU  - Ehsan,M
AU  - Du,Y
AU  - Mortensen,JS
AU  - Hariharan,P
AU  - Qu,Q
AU  - Ghani,L
AU  - Das,M
AU  - Grethen,A
AU  - Byrne,B
AU  - Skiniotis,G
AU  - Keller,S
AU  - Loland,CJ
AU  - Guan,L
AU  - Kobilka,BK
AU  - Chae,PS
DO  - 10.1002/chem.201902468
EP  - 11554
PY  - 2019///
SN  - 0947-6539
SP  - 11545
TI  - Self-assembly behavior and application of terphenyl-cored trimaltosides for membrane-protein studies: impact of detergent hydrophobic group geometry on protein stability
T2  - Chemistry - A European Journal
UR  - http://dx.doi.org/10.1002/chem.201902468
UR  - https://www.ncbi.nlm.nih.gov/pubmed/31243822
UR  - https://onlinelibrary.wiley.com/doi/full/10.1002/chem.201902468
UR  - http://hdl.handle.net/10044/1/72914
VL  - 25
ER  -
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