OmpF / OmpC - Outer Membrane Protein F and C
Family:
Outer membrane Channel Proteins, OMC family, β-Barrel and Porins Superfamily
Description:
OmpF and OmpC are two prokaryotic channel proteins which are located in the outer membrane and expressed amongst other bacteris by Escherichia coli, Salmonella typhimurium.
Topology and Function:
OmpF and OmpC forms pores that allow passive diffusion of small molecules across the outer membrane. Both are involved in osmoregulation: The widely distributed two-component system in bacteria, EnvZ/OmpR, respond to changes in envoronmental osmolality by regulating the expression of OmpF and OmpC the way that at lower osmolalities OmpC expression is less than OMPF expression.
Data and Applications
OmpF - Current block
Orbit mini and applications:
Data were kindly provided by Ionera.
Representative recording from a single OmpF trimer showing current blocks due to the translocation of antibiotic Enrofloxacin, event averaged histogram.
Conditions: 150 mM KCl, 5 mM HEPES, 5 mM MES, pH 6, 10 mM enrofloxacin, +60 mV
OmpF - Bilayer Recordings
Vesicle Prep Pro data and applications:
Data were kindly supplied by Prof. Mathias Winterhalter, Jacobs University, Bremen, Germany.
Channels were activated in the presence of spermine (0.5 mM). The downward spikes represent the closure events due to the effect of spermine.
Application Notes
OmpF - "Lipid Bilayer recordings of OmpF reconstituted in Proteoliposomes "
Port-a-Patch and Vesicle Prep Pro application note: 
(1.4 MB)
Posters
2016 - Parallel and automated formation of lipid bilayers on microstructured chips for ion channel and nanopore recordings
Orbit 16 poster (1.4 MB)
Kindly provided by Ionera Technologies
Publications
2020 - Electrophysiological characterization of transport across outer membrane channels from Gram‐negative bacteria in presence of lipopolysaccharides (LPS)
Port-a-Patch, 
Vesicle Prep Pro and 
Orbit mini Publication in Angewandte Chemie International Edition (2020)
Authors:
Wang J., Terrasse R., Bafna J.A., Benier L., Winterhalter M.
2018 - Quantifying Permeation of Small Charged Molecules across Channels: Electrophysiology in Small Volumes
Port-a-Patch and Vesicle Prep Pro publication in ACS Omega (2018)
Authors:
Wang J., Benier L., Winterhalter M.
2018 - Getting drugs into Gram-negative bacteria: Rational rules for permeation through general porins
Orbit 16 publication in ACS Infectious Diseases (2018)
Authors:
Acosta-Gutierrez S., Ferrara L., Pathania M., Masi M., Wang J., Bodrenko I., Zahn M., Winterhalter M., Stavenger R.A., Pages J.-M., Naismith J.H., van den Berg B., Page M., Ceccarelli M.
2015 - Quantification of Fluoroquinolone Uptake through the Outer Membrane Channel OmpF of Escherichia coli
Port-a-Patch and Vesicle Prep Pro publication in Journal of the American Chemical Society (2015)
Authors:
Cama J., Bajaj H., Pagliara S., Maier T., Braun Y., Winterhalter M., Keyser U.F.
2015 - Antibiotic translocation through porins studied in planar lipid bilayers using parallel platforms
Orbit 16, Port-a-Patch and Vesicle Prep Pro publication in Analyst (2015)
Authors:
Weichbrodt C., Bajaj H., Baaken G., Wang J., Guinot S., Kreir M, Behrends J.C., Winterhalter M., Fertig N.
2010 - Permeation of antibiotics through escherichia coli OmpF and OmpC porins: screening for influx on a single-molecule level
Port-a-Patch and Vesicle Prep Pro publication in Journal of Biomolecular Screening (2010)
Authors:
Mahendran K.R., Kreir M., Weingart H., Fertig N., Winterhalter M.
2009 - Port-a-Patch and Patchliner: High fidelity electrophysiology for secondary screening and safety pharmacology
Port-a-Patch and 
Patchliner publication in Combinatorial Chemistry & High Throughput Screening (2009)
Authors:
Farre C., Haythornthwaite A., Haarmann C., Stoelzle S., Kreir M., George M., Brüggemann A., Fertig N.
2008 - Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes
Port-a-Patch and Vesicle Prep Pro publication in Lab-on-a-chip (2008)
Authors:
Kreir M., Farre C., Beckler M., George M., Fertig N.