Single channel recordings of alpha-hemolysin reconstituted in S-layer-supported lipid bilayers.
Previous studies demonstrated that lipid membranes attached to a proteinaceous crystalline surface-layer (S-layer) revealed a prolonged lifetime and showed a reduced tendency to rupture in the presence of membrane active molecules. In addition, comparative studies on folded and S-layer-supported lipid membranes (SsLM) revealed an uniform capacitance of 0.64 +/- 0.04 microF/cm(2) for both composite membranes. In the present study, the feasibility to reconstitute the channel-forming protein alpha-hemolysin (alpha HL) into SsLM at single channel resolution was investigated. Single alpha HL channels could be recorded and the intrinsic properties like unitary conductance, current-voltage characteristics, and closure was found to be similar at both membranes. Thus, the tightly attached S-layer allowed complete reconstitution of alpha HL channels in SsLM.
Schuster
Bernhard
B
Center for Ultrastructure Research and Ludwig-Boltzmann-Institute for Molecular Nanotechnology, Universität für Bodenkultur Wien, Gregor Mendel Strasse 33, 1180 Vienna, Austria. bschuste@edv1.boku.ac.at
Sleytr
Uwe B
UB
D001426:Bacterial Proteins; D006460:Hemolysin Proteins / Q000737:chemistry*; D008051:Lipid Bilayers; D008564:Membrane Potentials; D009004:Monosaccharide Transport Proteins / Q000737:chemistry
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D008051:Lipid Bilayers; D009004:Monosaccharide Transport Proteins; C120455:SbpA protein, bacteria