| Literature DB >> 30969484 |
Muhammad Ehsan1,2, Ashwani Kumar1, Jonas S Mortensen3, Yang Du4, Parameswaran Hariharan5, Kaavya K Kumar4, Betty Ha4, Bernadette Byrne6, Lan Guan5, Brian K Kobilka4, Claus J Loland3, Pil Seok Chae1.
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 1 H 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.Entities:
Keywords: amphiphiles; membrane proteins; micelles; molecular design; protein stability; self-assembly
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Year: 2019 PMID: 30969484 PMCID: PMC7239035 DOI: 10.1002/asia.201900224
Source DB: PubMed Journal: Chem Asian J ISSN: 1861-471X