Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu 1-32 from HIV-1

Winfried Römer, Yuen H. Lam, Dahlia Fischer, Anthony Watts, Wolfgang B. Fischer, Petra Göring, Ralf B. Wehrspohn, Ulrich Gösele, Claudia Steinem*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

82 Scopus citations


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 μF/cm2. Membrane resistances were in the GΩ-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 Vpu1-32, which forms helix bundles with characteristic opening states. We elucidated different amilorides as potential drugs to inhibit channel activity of Vpu.

Original languageEnglish
Pages (from-to)16267-16274
Number of pages8
JournalJournal of the American Chemical Society
Issue number49
StatePublished - 15 Dec 2004


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