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{Sadaf:2017:10.1039/c7sc03700g,
author = {Sadaf, A and Du, Y and Santillan, C and Mortensen, JS and Molist, I and Seven, AB and Hariharan, P and Skiniotis, G and Loland, CJ and Kobilka, BK and Guan, L and Byrne, B and Chae, PS},
doi = {10.1039/c7sc03700g},
journal = {Chemical Science},
pages = {8315--8324},
title = {Dendronic trimaltoside amphiphiles (DTMs) for membrane protein study},
url = {http://dx.doi.org/10.1039/c7sc03700g},
volume = {8},
year = {2017}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The critical contribution of membrane proteins in normal cellular function makes their detailed structure and functional analysis essential. Detergents, amphipathic agents with the ability to maintain membrane proteins in a soluble state in aqueous solution, have key roles in membrane protein manipulation. Structural and functional stability is a prerequisite for biophysical characterization. However, many conventional detergents are limited in their ability to stabilize membrane proteins, making development of novel detergents for membrane protein manipulation an important research area. The architecture of a detergent hydrophobic group, that directly interacts with the hydrophobic segment of membrane proteins, is a key factor in dictating their efficacy for both membrane protein solubilization and stabilization. In the current study, we developed two sets of maltoside-based detergents with four alkyl chains by introducing dendronic hydrophobic groups connected to a trimaltoside head group, designated dendronic trimaltosides (DTMs). Representative DTMs conferred enhanced stabilization to multiple membrane proteins compared to the benchmark conventional detergent, DDM. One DTM (i.e., DTM-A6) clearly outperformed DDM in stabilizing human β2 adrenergic receptor (β2AR) and its complex with Gs protein. A further evaluation of this DTM led to a clear visualization of β2AR-Gs complex via electron microscopic analysis. Thus, the current study not only provides novel detergent tools useful for membrane protein study, but also suggests that the dendronic architecture has a role in governing detergent efficacy for membrane protein stabilization.
AU - Sadaf,A
AU - Du,Y
AU - Santillan,C
AU - Mortensen,JS
AU - Molist,I
AU - Seven,AB
AU - Hariharan,P
AU - Skiniotis,G
AU - Loland,CJ
AU - Kobilka,BK
AU - Guan,L
AU - Byrne,B
AU - Chae,PS
DO - 10.1039/c7sc03700g
EP - 8324
PY - 2017///
SN - 2041-6520
SP - 8315
TI - Dendronic trimaltoside amphiphiles (DTMs) for membrane protein study
T2 - Chemical Science
UR - http://dx.doi.org/10.1039/c7sc03700g
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000415877000052&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC03700G#!divAbstract
UR - http://hdl.handle.net/10044/1/76934
VL - 8
ER -