title: Reconstitution of purified VDAC1 into a lipid bilayer and recording of channel conductance.
abstract: The functional properties of purified voltage-dependent anion-selective channel protein 1 (VDAC1) have been examined in reconstituted systems based on artificially prepared phospholipid bilayers. The most widespread method for the characterization of the pore-forming activity of the mitochondrial VDAC1 protein requires reconstitution of the channel activity into a planar lipid bilayer (PLB) that separates two aqueous compartments. This system is able to produce a refined and large set of information on channel activity. The activity of the channel is reflected in the flow of ions (i.e., current) through a membrane that otherwise represents a barrier to ion flow. The setup thus requires the use of purified protein and a source of continuous current, as well as a sophisticated detector system able to amplify and record low, picoamper-level currents. This system is so efficient that the activity of even a single channel can be detected, allowing for study of VDAC1 at the molecular level.
authors.affiliation: Department of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
authors.forename: Danya
authors.initials: D
authors.lastname: Ben-Hail
authors.forename: Varda
authors.initials: V
authors.lastname: Shoshan-Barmatz
mesh_terms: D000818:Animals; D004560:Electricity; D007477:Ions / Q000378:metabolism; D008051:Lipid Bilayers / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology; D051336:Mitochondrial Membranes / Q000201:enzymology* / Q000502:physiology; D010539:Permeability; D051381:Rats; D050995:Voltage-Dependent Anion Channel 1 / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007477:Ions; D008051:Lipid Bilayers; C494764:Vdac1 protein, rat; D050995:Voltage-Dependent Anion Channel 1