NDLI: Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes

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Contents and Chemical Technology

Research Highlights ( Lab on a Chip Vol - 8 Issue - 4 )

Glass coating for PDMS microfluidic channels by sol–gel methods

Digital microfluidics for cell-based assays

Rapid, continuous purification of proteins in a microfluidic device using genetically-engineered partition tags

Artificial cilia for active micro-fluidic mixing

A polymer lab-on-a-chip for magnetic immunoassay with on-chip sampling and detection capabilities

Parasitic trap cancellation using multiple frequency dielectrophoresis, demonstrated by loading cells into cages

Experimental and model investigation of the time-dependent 2-dimensional distribution of binding in a herringbone microchannel

Model based design of a microfluidic mixer driven by induced charge electroosmosis

Electrokinetics induced asymmetric transport in polymeric nanonozzles

Nano-scale superhydrophobicity: suppression of protein adsorption and promotion of flow-induced detachment

Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes

Multiplexed proteomic sample preconcentration device using surface-patterned ion-selective membrane

Single molecule measurements within individual membrane-bound ion channels using a polymer-based bilayer lipid membrane chip

A low-cost, manufacturable method for fabricating capillary and optical fiber interconnects for microfluidic devices

Effect of the gelation process on the production of alginate microbeads by microfluidic chip technology

Shrinky-Dink microfluidics: 3D polystyrene chips

Non-equilibrium electrokinetic micro/nano fluidic mixer

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Lab on a Chip Vol - 8 Issue - 3

Lab on a Chip Vol - 8 Issue - 2

Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes

Content Provider	Royal Society of Chemistry (RSC)
Author	Farre, Cecilia Kreir, Mohamed Fertig, Niels George, Michael Beckler, Matthias
Copyright Year	2008
Abstract	Solvent-free planar lipid bilayers were formed in an automatic manner by bursting of giant unilamellar vesicles (GUVs) after gentle suction application through micron-sized apertures in a borosilicate glass substrate. Incubation of GUVs with the purified ion channel protein of interest yielded proteoliposomes. These proteoliposomes allow for immediate recording of channel activity after GUV sealing. This approach reduces the time-consuming, laborious and sometimes difficult protein reconstitution processes normally performed after bilayer formation. Bilayer recordings are attractive for investigations of membrane proteins not accessible to patch clamp analysis, like e.g.proteins from organelles. In the presented work, we show the example of the outer membrane protein OmpF from Escherichia coli. We reconstituted OmpF in proteoliposomes and observed the characteristic trimeric conductance levels and the typical gating induced by pH and transmembrane voltage. Moreover, OmpF is the main entrance for beta-lactam antibiotics and we investigated translocation processes of antibiotics and modulation of OmpF by spermine. We suggest that the rapid formation of porin containing lipid bilayers is of potential for the efficient electrophysiological characterization of the OmpF protein, for studying membrane permeation processes and for the rapid screening of antibiotics.
Starting Page	587
Ending Page	595
Page Count	9
File Format	HTM / HTML PDF
ISSN	14730197
Volume Number	8
Issue Number	4
Journal	Lab on a Chip
DOI	10.1039/b713982a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Membrane protein Beta-lactam Spermine General Utility Van Escherichia coli Patch clamp PH Ion Borosilicate glass Porin (protein) Lipid Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry Nanoscience and Nanotechnology Biochemistry Bioengineering Biomedical Engineering

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PAPER www.rsc.org/loc Lab on a Chip Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes (2008)

Deletions of single extracellular loops affect pH sensitivity, but not voltage dependence, of the Escherichia coli porin OmpF

Mutants of Escherichia coli That Are Resistant to Certain Beta-Lactam Compounds Lack the ompF Porin

Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli (1991)

A Novel Regulatory Cascade Involving BluR, YcgZ, and Lon Controls the Expression of Escherichia coli OmpF Porin

Overexpression of parathion hydrolase in Escherichia coli stimulates the synthesis of outer membrane porin OmpF

Role of Auxiliary Membrane Components in Beta-Lactam Antibiotic Sensitivity of Escherichia coli

Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.

Regulation of OmpF porin expression by salicylate in Escherichia coli (1991)

Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes

Similar Documents

PAPER www.rsc.org/loc Lab on a Chip Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes (2008)

Deletions of single extracellular loops affect pH sensitivity, but not voltage dependence, of the Escherichia coli porin OmpF

Mutants of Escherichia coli That Are Resistant to Certain Beta-Lactam Compounds Lack the ompF Porin

Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli (1991)

A Novel Regulatory Cascade Involving BluR, YcgZ, and Lon Controls the Expression of Escherichia coli OmpF Porin

Overexpression of parathion hydrolase in Escherichia coli stimulates the synthesis of outer membrane porin OmpF

Role of Auxiliary Membrane Components in Beta-Lactam Antibiotic Sensitivity of Escherichia coli

Primary structure of major outer-membrane protein I (ompF protein, porin) of Escherichia coli B/r.

Regulation of OmpF porin expression by salicylate in Escherichia coli (1991)

Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes