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Self-Assembly Behaviors of a Penta-Phenylene Maltoside and Its Application for Membrane Protein Study.

Research paper by Muhammad M Ehsan, Ashwani A Kumar, Jonas S JS Mortensen, Yang Y Du, Parameswaran P Hariharan, Kaavya K KK Kumar, Betty B Ha, Bernadette B Byrne, Lan L Guan, Brian K BK Kobilka, Claus J CJ Loland, Pil Seok PS Chae

Indexed on: 12 Apr '19Published on: 11 Apr '19Published in: Chemistry - An Asian Journal



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 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. © 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.