A New Class of Amphiphiles Bearing Rigid Hydrophobic Groups for Solubilization and Stabilization of Membrane Proteins
- Authors
- Chae, Pil Seok; Rasmussen, Soren G. F.; Rana, Rohini R.; Gotfryd, Kamil; Kruse, Andrew C.; Manglik, Aashish; Cho, Kyung Ho; Nurva, Shailika; Gether, Ulrik; Guan, Lan; Loland, Claus J.; Byrne, Bernadette; Kobilka, Brian K.; Gellman, Samuel H.
- Issue Date
- Jul-2012
- Publisher
- John Wiley & Sons Ltd.
- Keywords
- amphiphiles; membrane proteins; molecular design; solubilization; stabilization
- Citation
- Chemistry - A European Journal, v.18, no.31, pp.9485 - 9490
- Indexed
- SCIE
SCOPUS
- Journal Title
- Chemistry - A European Journal
- Volume
- 18
- Number
- 31
- Start Page
- 9485
- End Page
- 9490
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/32271
- DOI
- 10.1002/chem.201200069
- ISSN
- 0947-6539
- Abstract
- Non-traditional amphiphiles: Conferring aqueous solubility on membrane proteins generally requires the use of a detergent or other amphiphilic agent. A new class of amphiphiles was synthesized, based on steroidal lipophilic groups, and evaluated with several membrane proteins. The results show that the new amphiphile, "glyco-diosgenin" (GDN; see figure), confers enhanced stability to a variety of membrane proteins in solution relative to popular conventional detergents, such as dodecylmaltoside (DDM). Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles
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