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    Minimal F-Actin Cytoskeletal System for Planar Supported Phospholipid Bilayers

    Year: 2008

    Journal: Langmuir 2008, 24, 6827-6836., 20100827

    Authors: Barfoot R.J., Sheikh K.H., Johnson B.R.J, Colyer J., Miles R.E., Jeuken L.J.C., Bushby R.J., Evans S.D.

    Last authors: Stephen D. Evans

    Organizations: School of Physics and Astronomy, Center for Self-Organizing Molecular Systems, and School of Electronic and Electrical Engineering, UniVersity of Leeds, Leeds, LS2 9JT, United Kingdom

    Country: UK, United Kingdom

    Preferential binding of F-actin to lipid bilayers containing ponticulin was investigated on both planar supported bilayers and on a cholesterol-based tethering system. The transmembrane protein ponticulin in Dictyostelium discoideum is known to provide a direct link between the actin cytoskeleton and the cell membrane (Wuestehube, L. J.; Luna, E. J. J. Cell Biol. 1987, 105, 1741-1751). Purification of ponticulin has allowed an in vitro model of the F-actin cytoskeletal scaffold system to be formed and investigated by AFM, epi- fluorescence microscopy, surface plasmon resonance (SPR), and quartz crystal microbalance with dissipation (QCM-D). Single filament features of F-actin bound to the ponticulin containing lipid bilayer are shown by AFM to have a pitch of 37.3 ( 1.1 nm and a filament height of 7.0 ( 1.6 nm. The complementary techniques of QCM-D and SPR were used to obtain dissociation constants for the interaction of F-actin with ponticulin containing bilayers, giving 10.5 ( 1.7 μM for a physisorbed bilayer and 10.8 ( 3.6 μM for a tethered bilayer, respectively.