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Dendronic trimaltoside amphiphiles (DTMs) for membrane protein study

Title
Dendronic trimaltoside amphiphiles (DTMs) for membrane protein study
Author
채필석
Keywords
GLYCOL GNG AMPHIPHILES; CRYSTAL-STRUCTURE; BETA(2)-ADRENERGIC RECEPTOR; MNG AMPHIPHILES; SOLUBILIZATION; STABILIZATION; CRYSTALLIZATION; FLUORESCENCE; DETERGENTS; STABILITY
Issue Date
2017-12
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL SCIENCE, v. 8, no. 12, page. 8315-8324
Abstract
The critical contribution of membrane proteins in normal cellular function makes their detailed structure and functional analysis essential. Detergents, amphipathic agents with the ability to maintain membrane proteins in a soluble state in aqueous solution, have key roles in membrane protein manipulation. Structural and functional stability is a prerequisite for biophysical characterization. However, many conventional detergents are limited in their ability to stabilize membrane proteins, making development of novel detergents for membrane protein manipulation an important research area. The architecture of a detergent hydrophobic group, that directly interacts with the hydrophobic segment of membrane proteins, is a key factor in dictating their efficacy for both membrane protein solubilization and stabilization. In the current study, we developed two sets of maltoside-based detergents with four alkyl chains by introducing dendronic hydrophobic groups connected to a trimaltoside head group, designated dendronic trimaltosides (DTMs). Representative DTMs conferred enhanced stabilization to multiple membrane proteins compared to the benchmark conventional detergent, DDM. One DTM (i.e., DTM-A6) clearly outperformed DDM in stabilizing human beta(2) adrenergic receptor (beta(2)AR) and its complex with G(s) protein. A further evaluation of this DTM led to a clear visualization of beta(2)AR-G(s) complex via electron microscopic analysis. Thus, the current study not only provides novel detergent tools useful for membrane protein study, but also suggests that the dendronic architecture has a role in governing detergent efficacy for membrane protein stabilization.
URI
https://pubs.rsc.org/en/content/articlelanding/2017/SC/C7SC03700G#!divAbstracthttp://repository.hanyang.ac.kr/handle/20.500.11754/116840
ISSN
2041-6520; 2041-6539
DOI
10.1039/c7sc03700g
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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