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Hydrophobic Variations of N-Oxide Amphiphiles for Membrane Protein Manipulation: Importance of Non-hydrocarbon Groups in the Hydrophobic Portion

Title
Hydrophobic Variations of N-Oxide Amphiphiles for Membrane Protein Manipulation: Importance of Non-hydrocarbon Groups in the Hydrophobic Portion
Author
채필석
Keywords
amphiphiles; membrane proteins; molecular design; non-hydrocarbon groups; stabilization
Issue Date
2014-01
Publisher
WILEY-V C H VERLAG GMBH, BOSCHSTRASSE 12, D-69469 WEINHEIM, GERMANY
Citation
CHEMISTRY-AN ASIAN JOURNAL, JAN 2014, 9(1), p110-p116, 7p.
Abstract
Amphipathic agents called detergents serve as membrane-mimetic systems to maintain the native structures of membrane proteins during their manipulation. However, membrane proteins solubilized in conventional detergents tend to undergo denaturation and aggregation, necessitating the development of novel amphipathic agents with enhanced properties. Here we describe several new amphiphiles that contain an N-oxide group as the hydrophilic portion. The new amphiphiles have been evaluated for the ability to solubilize and stabilize a fragile multi-subunit assembly from biological membranes. We found that cholate-based agents were promising in supporting retention of the native protein quaternary structure, while deoxycholate-based amphiphiles were highly efficient in extracting/solubilizing the intact superassembly from the native membrane. Monitoring superassembly solubilization and stabilization as a function of variation in amphiphile structure led us to propose that a non-hydrocarbon moiety such as an amide, ether, or a hydroxy group present in the lipophilic regions can manifest distinctive effects in the context of membrane protein manipulation.
URI
http://onlinelibrary.wiley.com/doi/abs/10.1002/asia.201301097http://hdl.handle.net/20.500.11754/53810
ISSN
1861-4728
DOI
10.1002/asia.201301097
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GRADUATE SCHOOL[S](대학원) > ETC
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