Imperial College London

ProfessorBernadetteByrne

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology
 
 
 
//

Contact

 

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

 
 
//

Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Ehsan:2018:10.1039/c8ob00270c,
author = {Ehsan, M and Du, Y and Molist, I and Seven, AB and Hariharan, P and Mortensen, JS and Ghani, L and Loland, CJ and Skiniotis, G and Guan, L and Byrne, B and Kobilka, BK and Chae, PS},
doi = {10.1039/c8ob00270c},
journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
pages = {2489--2498},
title = {Vitamin E-based glycoside amphiphiles for membrane protein structural studies},
url = {http://dx.doi.org/10.1039/c8ob00270c},
volume = {16},
year = {2018}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Membrane proteins play critical roles in a variety of cellular processes. For a detailed molecular level understanding of their biological functions and roles in disease, it is necessary to extract them from the native membranes. While the amphipathic nature of these bio-macromolecules presents technical challenges, amphiphilic assistants such as detergents serve as useful tools for membrane protein structural and functional studies. Conventional detergents are limited in their ability to maintain the structural integrity of membrane proteins and thus it is essential to develop novel agents with enhanced properties. Here, we designed and characterized a novel class of amphiphiles with vitamin E (i.e., α-tocopherol) as the hydrophobic tail group and saccharide units as the hydrophilic head group. Designated vitamin E-based glycosides (VEGs), these agents were evaluated for their ability to solubilize and stabilize a set of membrane proteins. VEG representatives not only conferred markedly enhanced stability to a diverse range of membrane proteins compared to conventional detergents, but VEG-3 also showed notable efficacy toward stabilization and visualization of a membrane protein complex. In addition to hydrophile–lipophile balance (HLB) of detergent molecules, the chain length and molecular geometry of the detergent hydrophobic group seem key factors in determining detergent efficacy for membrane protein (complex) stability.
AU - Ehsan,M
AU - Du,Y
AU - Molist,I
AU - Seven,AB
AU - Hariharan,P
AU - Mortensen,JS
AU - Ghani,L
AU - Loland,CJ
AU - Skiniotis,G
AU - Guan,L
AU - Byrne,B
AU - Kobilka,BK
AU - Chae,PS
DO - 10.1039/c8ob00270c
EP - 2498
PY - 2018///
SN - 1477-0520
SP - 2489
TI - Vitamin E-based glycoside amphiphiles for membrane protein structural studies
T2 - ORGANIC & BIOMOLECULAR CHEMISTRY
UR - http://dx.doi.org/10.1039/c8ob00270c
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000429204000016&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/59059
VL - 16
ER -