Imperial College London
Portrait Picture

ProfessorBernadetteByrne

Faculty of Natural Sciences, Department of Life Sciences

Associate Dean (Equality, Diversity and Inclusion) for FoNS
 
 
 
//

Contact

 

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

 
 
//

Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Ghani:2022:10.1002/chem.202200116,
author = {Ghani, L and Kim, S and Wang, H and Lee, HS and Mortensen, JS and Katsube, S and Du, Y and Sadaf, A and Ahmed, W and Byrne, B and Guan, L and Loland, CJ and Kobilka, BK and Im, W and Chae, PS},
doi = {10.1002/chem.202200116},
journal = {Chemistry: A European Journal},
title = {Foldable detergents for membrane protein study: importance of setergent core flexibility in protein stabilization.},
url = {http://dx.doi.org/10.1002/chem.202200116},
year = {2022}
}
Download

RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Membrane proteins are of biological and pharmaceutical significance. However, their structural study is extremely challenging mainly due to the fact that only a small number of chemical tools are suitable for stabilizing membrane proteins in solution. Detergents are widely used in membrane protein study, but conventional detergents are generally poor at stabilizing challenging membrane proteins such as G protein-coupled receptors and protein complexes. In the current study, we prepared tandem triazine-based maltosides (TZMs) with two amphiphilic triazine units connected by different diamine linkers, hydrazine (TZM-Hs) and 1,2-ethylenediamine (TZM-Es). These TZMs were consistently superior to a gold standard detergent (DDM) in terms of stabilizing a few membrane proteins. In addition, the TZM-Es containing a long linker showed more general protein stabilization efficacy with multiple membrane proteins than the TZM-Hs containing a short linker. This result indicates that introduction of the flexible1,2-ethylenediamine linker between two rigid triazine rings enables the TZM-Es to fold into favourable conformations in order to promote membrane protein stability. The novel concept of detergent foldability introduced in the current study has potential in rational detergent design and membrane protein applications.
AU  - Ghani,L
AU  - Kim,S
AU  - Wang,H
AU  - Lee,HS
AU  - Mortensen,JS
AU  - Katsube,S
AU  - Du,Y
AU  - Sadaf,A
AU  - Ahmed,W
AU  - Byrne,B
AU  - Guan,L
AU  - Loland,CJ
AU  - Kobilka,BK
AU  - Im,W
AU  - Chae,PS
DO  - 10.1002/chem.202200116
PY  - 2022///
SN  - 0947-6539
TI  - Foldable detergents for membrane protein study: importance of setergent core flexibility in protein stabilization.
T2  - Chemistry: A European Journal
UR  - http://dx.doi.org/10.1002/chem.202200116
UR  - https://www.ncbi.nlm.nih.gov/pubmed/35238091
UR  - https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202200116
ER  -
Download