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An Engineered Lithocholate-Based Facial Amphiphile Stabilizes Membrane Proteins: Assessing the Impact of Detergent Customizability on Protein Stability

Title
An Engineered Lithocholate-Based Facial Amphiphile Stabilizes Membrane Proteins: Assessing the Impact of Detergent Customizability on Protein Stability
Author
채필석
Keywords
amphiphiles; membrane proteins; micelles; protein stabilization; protein structures
Issue Date
2018-07
Publisher
WILEY-V C H VERLAG GMBH
Citation
CHEMISTRY-A EUROPEAN JOURNAL, v. 24, no. 39, page. 9860-9868
Abstract
Amphiphiles are critical tools for the structural and functional study of membrane proteins. Membrane proteins encapsulated by conventional head-to-tail detergents tend to undergo structural degradation, necessitating the development of structurally novel agents with improved efficacy. In recent years, facial amphiphiles have yielded encouraging results in terms of membrane protein stability. Herein, we report a new facial detergent (i.e., LFA-C4) that confers greater stability to tested membrane proteins than the bola form analogue. Owing to the increased facial property and the adaptability of the detergent micelles in complex with different membrane proteins, LFA-C4 yields increased stability compared to n-dodecyl-beta-D-maltoside (DDM). Thus, this study not only describes a novel maltoside detergent with enhanced protein-stabilizing properties, but also shows that the customizable nature of a detergent plays an important role in the stabilization of membrane proteins. Owing to both synthetic convenience and enhanced stabilization efficacy for a range of membrane proteins, the new agent has major potential in membrane protein research.
URI
https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.201801141https://repository.hanyang.ac.kr/handle/20.500.11754/119382
ISSN
0947-6539; 1521-3765
DOI
10.1002/chem.201801141
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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