Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study

Title
Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study
Authors
김진웅
Keywords
MUSCARINIC ACETYLCHOLINE-RECEPTOR; CRYSTAL-STRUCTURE; FACIAL AMPHIPHILES; AQUEOUS-SOLUTIONS; COUPLED RECEPTOR; GNG AMPHIPHILES; STABILIZATION; DETERGENT; SOLUBILIZATION; CRYSTALLIZATION
Issue Date
2015-05
Publisher
ROYAL SOC CHEMISTRY
Citation
ANALYST, v. 140, Page. 3157-3163
Abstract
Detergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to ˃10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-beta-D-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.
URI
http://pubs.rsc.org/en/Content/ArticleLanding/2015/AN/C5AN00240Khttp://hdl.handle.net/20.500.11754/24787
ISSN
0003-2654; 1364-5528
DOI
http://dx.doi.org/10.1039/c5an00240k
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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