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{Hussain:2017:10.1002/chem.201605016,
author = {Hussain, H and Du, Y and Tikhonova, E and Mortensen, JS and Ribeiro, O and Santillan, C and Das, M and Ehsan, M and Loland, CJ and Guan, L and Kobilka, BK and Byrne, B and Chae, PS},
doi = {10.1002/chem.201605016},
journal = {CHEMISTRY-A EUROPEAN JOURNAL},
pages = {6724--6729},
title = {Resorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stability},
url = {http://dx.doi.org/10.1002/chem.201605016},
volume = {23},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - As a membrane-mimetic system, detergent micelles are popularly used to extract membrane proteins from lipid environments and to maintain their solubility and stability in an aqueous medium. However, many membrane proteins encapsulated in conventional detergents tend to undergo structural degradation during extraction and purification, thus necessitating the development of new agents with enhanced properties. In the current study, two classes of new amphiphiles are introduced, resorcinarene-based glucoside and maltoside amphiphiles (designated RGAs and RMAs, respectively), for which the alkyl chains are facially segregated from the carbohydrate head groups. Of these facial amphiphiles, two RGAs (RGA-C11 and RGA-C13) conferred markedly enhanced stability to four tested membrane proteins compared to a gold-standard conventional detergent. The relatively high water solubility and micellar stability of the RGAs compared to the RMAs, along with their generally favourable behaviours for membrane protein stabilisation described here, are likely to be, at least in part, a result of the high conformational flexibility of these glucosides. This study suggests that flexibility could be an important factor in determining the suitability of new detergents for membrane protein studies.
AU  - Hussain,H
AU  - Du,Y
AU  - Tikhonova,E
AU  - Mortensen,JS
AU  - Ribeiro,O
AU  - Santillan,C
AU  - Das,M
AU  - Ehsan,M
AU  - Loland,CJ
AU  - Guan,L
AU  - Kobilka,BK
AU  - Byrne,B
AU  - Chae,PS
DO  - 10.1002/chem.201605016
EP  - 6729
PY  - 2017///
SN  - 0947-6539
SP  - 6724
TI  - Resorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stability
T2  - CHEMISTRY-A EUROPEAN JOURNAL
UR  - http://dx.doi.org/10.1002/chem.201605016
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000401573100004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/48825
VL  - 23
ER  -
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