Self-Assembly Behaviors of a Penta-Phenylene Maltoside and Its Application for Membrane Protein Study
- Authors
- Ehsan, Muhammad; Kumar, Ashwani; Mortensen, Jonas S.; Du, Yang; Hariharan, Parameswaran; Kumar, Kaavya K.; Ha, Betty; Byrne, Bernadette; Guan, Lan; Kobilka, Brian K.; Loland, Claus J.; Chae, Pil Seok
- Issue Date
- Jun-2019
- Publisher
- Wiley - V C H Verlag GmbbH & Co.
- Keywords
- amphiphiles; membrane proteins; micelles; molecular design; protein stability; self-assembly
- Citation
- Chemistry - An Asian Journal, v.14, no.11, pp.1926 - 1931
- Indexed
- SCIE
SCOPUS
- Journal Title
- Chemistry - An Asian Journal
- Volume
- 14
- Number
- 11
- Start Page
- 1926
- End Page
- 1931
- URI
- https://scholarworks.bwise.kr/erica/handle/2021.sw.erica/2842
- DOI
- 10.1002/asia.201900224
- ISSN
- 1861-4728
- Abstract
- We prepared an amphiphile with a penta-phenylene lipophilic group and a branched trimaltoside head group. This new agent, designated penta-phenylene maltoside (PPM), showed a marked tendency to self-assembly into micelles via strong aromatic-aromatic interactions in aqueous media, as evidenced by H-1 NMR spectroscopy and fluorescence studies. When utilized for membrane protein studies, this new agent was superior to DDM, a gold standard conventional detergent, in stabilizing multiple proteins long term. The ability of this agent to form aromatic-aromatic interactions is likely responsible for enhanced protein stabilization when associated with a target membrane protein.
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Collections - COLLEGE OF ENGINEERING SCIENCES > DEPARTMENT OF BIONANO ENGINEERING > 1. Journal Articles
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