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New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies

Title
New penta-saccharide-bearing tripod amphiphiles for membrane protein structure studies
Author
채필석
Keywords
CRYSTAL-STRUCTURE; FACIAL AMPHIPHILES; MNG AMPHIPHILES; CRYSTALLIZATION; STABILIZATION; RECEPTOR; SOLUBILIZATION; DETERGENTS; INSIGHTS; BINDING
Issue Date
2017-10
Publisher
ROYAL SOC CHEMISTRY
Citation
ANALYST, v. 142, no. 20, page. 3889-3898
Abstract
Integral membrane proteins either alone or as complexes carry out a range of key cellular functions. Detergents are indispensable tools in the isolation of membrane proteins from biological membranes for downstream studies. Although a large number of techniques and tools, including a wide variety of detergents, are available, purification and structural characterization of many membrane proteins remain challenging. In the current study, a new class of tripod amphiphiles bearing two different penta-saccharide head groups, designated TPSs, were developed and evaluated for their ability to extract and stabilize a range of diverse membrane proteins. Variations in the structures of the detergent head and tail groups allowed us to prepare three sets of the novel agents with distinctive structures. Some TPSs (TPS-A8 and TPS-E7) were efficient at extracting two proteins in a functional state while others (TPS-E8 and TPS-E10L) conferred marked stability to all membrane proteins (and membrane protein complexes) tested here compared to a conventional detergent. Use of TPS-E10L led to clear visualization of a receptor-Gs complex using electron microscopy, indicating profound potential in membrane protein research.
URI
https://pubs.rsc.org/en/content/articlelanding/2017/AN/C7AN01168G#!divAbstracthttp://repository.hanyang.ac.kr/handle/20.500.11754/115827
ISSN
0003-2654; 1364-5528
DOI
10.1039/c7an01168g
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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