Imperial College London


Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology



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




504Sir Ernst Chain BuildingSouth Kensington Campus






BibTex format

author = {Ghani, L and Munk, CF and Zhang, X and Katsube, S and Du, Y and Cecchetti, C and Huang, W and Bae, HE and Saouros, S and Ehsan, M and Guan, L and Liu, X and Loland, CJ and Kobilka, BK and Byrne, B and Chae, PS},
doi = {10.1021/jacs.9b07883},
journal = {Journal of the American Chemical Society},
pages = {19677--19687},
title = {1,3,5-Triazine-cored maltoside amphiphiles for membrane protein extraction and stabilization},
url = {},
volume = {141},
year = {2019}

RIS format (EndNote, RefMan)

AB - Despite their major biological and pharmacological significance, the structural and functional study of membrane proteins remains a significant challenge. A main issue is the isolation of these proteins in a stable and functional state from native lipid membranes. Detergents are amphiphilic compounds widely used to extract membrane proteins from the native membranes and maintain them in a stable form during downstream analysis. However, due to limitations of conventional detergents, it is essential to develop novel amphiphiles with optimal properties for protein stability in order to advance membrane protein research. Here we designed and synthesized 1,3,5-triazine-cored dimaltoside amphiphiles derived from cyanuric chloride. By introducing variations in the alkyl chain linkage (ether/thioether) and an amine-functionalized diol linker (serinol/diethanolamine), we prepared two sets of 1,3,5-triazine-based detergents. When tested with several model membrane proteins, these agents showed remarkable efficacy in stabilizing three transporters and two G protein-coupled receptors. Detergent behavior substantially varied depending on the detergent structural variation, allowing us to explore detergent structure–property–efficacy relationships. The 1,3,5-triazine-based detergents introduced here have significant potential for membrane protein study as a consequence of their structural diversity and universal stabilization efficacy for several membrane proteins.
AU - Ghani,L
AU - Munk,CF
AU - Zhang,X
AU - Katsube,S
AU - Du,Y
AU - Cecchetti,C
AU - Huang,W
AU - Bae,HE
AU - Saouros,S
AU - Ehsan,M
AU - Guan,L
AU - Liu,X
AU - Loland,CJ
AU - Kobilka,BK
AU - Byrne,B
AU - Chae,PS
DO - 10.1021/jacs.9b07883
EP - 19687
PY - 2019///
SN - 0002-7863
SP - 19677
TI - 1,3,5-Triazine-cored maltoside amphiphiles for membrane protein extraction and stabilization
T2 - Journal of the American Chemical Society
UR -
UR -
UR -
VL - 141
ER -