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Voltage-Dependent Anion Channel Transports Calcium Ions through Biomimetic Membranes

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    Research Article

    Voltage-Dependent Anion Channel Transports Calcium Ions through Biomimetic Membranes
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    CNRS UMR 8159, Laboratoire de Génétique et Biologie Cellulaire, Université de Versailles/St Quentin, 45 Avenue des Etats-Unis, 78035 Versailles, France, UMR 6022 CNRS, Université de Technologie de Compiègne, BP 20529, 60205 Compiègne cedex, France, UMR-CNRS 168 and LRC-CEA 34V, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France, Max-Planck Institut für Polymerforschung, Ackermannweg 10, 55128 Mainz, Germany, and CNRS UMR 5048, Centre de Biochimie Structurale, INSERM U554, and Université Montpellier 1 et 2, F34090 Montpellier, France
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    Langmuir

    Cite this: Langmuir 2007, 23, 7, 3898–3905
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    https://doi.org/10.1021/la063105+
    Published February 22, 2007
    Copyright © 2007 American Chemical Society
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    Abstract

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    The mitochondrial outer membrane channel (VDAC), a central player in mitochondria and cell death, was reconstituted in polymer-supported phospholipid bilayers. Highly purified VDAC was first reconstituted in vesicles; channel properties and NADH-ferricyanide reductase activity were ascertained before deposition onto solid substrates. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/1,2-distearoyl-sn-glycero-3-phosphoethanolamine−poly(ethylene glycol)−N-hydroxysuccinimide mixed vesicles containing VDAC were linked onto amine-grafted surfaces (glass and gold) and disrupted to form a VDAC-containing polymer-tethered planar bilayer. Surface plasmon spectroscopy, fluorescence microscopy, and atomic force microscopy measurements ascertained the membrane thickness, fluidity, and continuity. VDAC reconstituted in bilayers efficiently transported calcium ions and was modulable by two channel blockers, 4,4‘-diisothiocyanatostilbene-2,2‘-disulfonic acid and l-glutamate. The novel setup may allow the study of the assembly of a polyprotein complex centered on VDAC and its role in mitochondrial biology, calcium fluxes, and apoptosis.

    Copyright © 2007 American Chemical Society

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    †

     Université de Versailles/St Quentin.

    ‡

     Université de Technologie de Compiègne.

    §

     UMR-CNRS 168 and LRC-CEA 34V.

    ⊥

     Centre de Biochimie Structurale, INSERM U554, and Université Montpellier 1 et 2.

    ‖

     Max-Planck Institut für Polymerforschung.

    *

     To whom correspondence should be addressed. E-mail:  [email protected].

    Cited By

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    This article is cited by 44 publications.

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    Langmuir

    Cite this: Langmuir 2007, 23, 7, 3898–3905
    Click to copy citationCitation copied!
    https://doi.org/10.1021/la063105+
    Published February 22, 2007
    Copyright © 2007 American Chemical Society
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