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Glycotripod amphiphiles for solubilization and stabilization of a membrane-protein superassembly: Importance of branching in the hydrophilic portion

Authors
Chae,Pil-seokWander, Marc J.Bowling, Aaron P.Laible, Philip D.Gellman, Samuel H.
Issue Date
Jul-2008
Publisher
John Wiley & Sons Ltd.
Keywords
amphiphiles; detergent design; membrane proteins; solubilization; stabilization
Citation
ChemBioChem, v.9, no.11, pp.1706 - 1709
Indexed
SCIE
SCOPUS
Journal Title
ChemBioChem
Volume
9
Number
11
Start Page
1706
End Page
1709
URI
https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/42273
DOI
10.1002/cbic.200800169
ISSN
1439-4227
Abstract
Three-legged friends: Intrinsic membrane proteins must usually be extracted from the native membrane with the aid of synthetic amphiphiles and then stabilized before detailed structural and functional characterization is possible. We describe new amphiphiles with unusual architectures that were useful for extraction and stabilization of protein superassemblies from bacterial membranes. Our results suggest that incorporation of branch points (as shown in figure) in both the hydrophilic and lipophilic portions can lead to favorable amphiphile behavior.
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COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles

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ERICA 공학대학 (DEPARTMENT OF BIONANO ENGINEERING)
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