title: Channel activity of OmpF monitored in nano-BLMs.
abstract: Free-standing lipid bilayer membranes can be formed on small apertures (60 nm diameter) on highly ordered porous alumina substrates. The formation process of the membranes on a 1,2-dipalmitoyl-sn-glycero-3-phosphothioethanol submonolayer was followed by impedance spectroscopy. After lipid bilayers had thinned, the reconstitution and ionic conducting properties of the outer membrane protein OmpF of E. coli were monitored using single-channel recordings. The characteristic conductance states of the three monomers, fast kinetics, and subconductance states were observed. Blockade of the ion flow as a result of interaction of the antibiotic ampicillin with the protein was verified, indicating the full functionality of the protein channel in nanometer-scale bilayer membranes.
authors.affiliation: Institut für Analytische Chemie, Chemo- und Biosensorik, Universität Regensburg, 93040 Regensburg, Germany.
authors.forename: Eva K
authors.initials: EK
authors.lastname: Schmitt
authors.forename: Maarten
authors.initials: M
authors.lastname: Vrouenraets
authors.forename: Claudia
authors.initials: C
authors.lastname: Steinem
mesh_terms: D000537:Aluminum Oxide / Q000737:chemistry; D000667:Ampicillin / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D015640:Ion Channel Gating; D008051:Lipid Bilayers / Q000737:chemistry*; D049329:Nanostructures; D010712:Phosphatidic Acids / Q000737:chemistry; D018272:Porins / Q000737:chemistry*; D013057:Spectrum Analysis
chemical_list: C104363:1,2-dipalmitoyl-sn-glycero-3-phosphatidylethanol; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; C109237:OmpF protein; D010712:Phosphatidic Acids; D018272:Porins; D000667:Ampicillin; D000537:Aluminum Oxide