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  • Title: Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu(1-32) from HIV-1.
    Author: Römer W, Lam YH, Fischer D, Watts A, Fischer WB, Göring P, Wehrspohn RB, Gösele U, Steinem C.
    Journal: J Am Chem Soc; 2004 Dec 15; 126(49):16267-74. PubMed ID: 15584764.
    Abstract:
    We report for the first time on pore-suspending lipid bilayers, which we call micro-black lipid membranes (micro-BLMs), based on a highly ordered macroporous silicon array. Micro-BLMs were established by first functionalizing the backside porous silicon surface with gold and then chemisorbing 1,2-dipalmitoyl-sn-glycero-3-phosphothioethanol followed by spreading 1,2-diphytanoyl-sn-glycero-3-phosphocholine dissolved in n-decane. Impedance spectroscopy revealed the formation of single lipid bilayers confirmed by a mean specific capacitance of 0.6 +/- 0.2 microF/cm2. Membrane resistances were in the G omega-regime and beyond. The potential of the system for single channel recordings was demonstrated by inserting the transmembrane domain of the HIV-1 accessory peptide Vpu(1-32), which forms helix bundles with characteristic opening states. We elucidated different amilorides as potential drugs to inhibit channel activity of Vpu.
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