Asymmetric maltose neopentyl glycol amphiphiles for a membrane protein study: effect of detergent asymmetricity on protein stabilityopen access
- Authors
- Bae, Hyoung Eun; Du, Yang; Hariharan, Parameswaran; Mortensen, Jonas S.; Kumar, Kaavya K.; Ha, Betty; Das, Manabendra; Lee, Hyun Sung; Loland, Claus J.; Guan, Lan; Kobilka, Brian K.; Chae, Pil Seok
- Issue Date
- Jan-2019
- Publisher
- Royal Society of Chemistry
- Citation
- Chemical Science, v.10, no.4, pp.1107 - 1116
- Indexed
- SCIE
SCOPUS
- Journal Title
- Chemical Science
- Volume
- 10
- Number
- 4
- Start Page
- 1107
- End Page
- 1116
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/3556
- DOI
- 10.1039/c8sc02560f
- ISSN
- 2041-6520
- Abstract
- Maintaining protein stability in an aqueous solution is a prerequisite for protein structural and functional studies, but conventional detergents have increasingly showed limited ability to maintain protein integrity. A representative novel agent, maltose neopentyl glycol-3 (MNG-3), has recently substantially contributed to membrane protein structural studies. Motivated by the popular use of this novel agent, we prepared asymmetric versions of MNG-3 and evaluated these agents with several membrane proteins including two G protein-coupled receptors in this study. We found that some new MNGs were significantly more effective than MNG-3 at preserving protein integrity in the long term, suggesting that these asymmetric MNGs will find a wide use in membrane protein studies. In addition, this is the first study addressing the favorable effect of detergent asymmetric nature on membrane protein stability.
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Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles
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