Resorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stability
File(s)
Accepted version
Author(s)
Type
Journal Article
Abstract
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.
Date Issued
2017-04-20
Date Acceptance
2017-03-17
Citation
CHEMISTRY-A EUROPEAN JOURNAL, 2017, 23 (28), pp.6724-6729
ISSN
0947-6539
Publisher
WILEY
Start Page
6724
End Page
6729
Journal / Book Title
CHEMISTRY-A EUROPEAN JOURNAL
Volume
23
Issue
28
Copyright Statement
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the accepted version of the following article: H. Hussain, Y. Du, E. Tikhonova, J. S. Mortensen, O. Ribeiro, C. Santillan, M. Das, M. Ehsan, C. J. Loland, L. Guan, B. K. Kobilka, B. Byrne, P. S. Chae, Chem. Eur. J. 2017, 23, 6724, which has been published in final form at https://dx.doi.org/10.1002/chem.201605016
Identifier
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000401573100004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
Subjects
Science & Technology
Physical Sciences
Chemistry, Multidisciplinary
Chemistry
facial amphiphiles
membrane proteins
molecular design
protein stability
resorcinarene glycosides
AQUEOUS-SOLUTIONS
AMPHIPHILES
STABILIZATION
SOLUBILIZATION
CRYSTALLIZATION
SURFACTANTS
NANODISCS
TRANSPORT
AMPHIPOLS
General Chemistry
03 Chemical Sciences
Publication Status
Published