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

J Am Chem Soc. 2004 Dec 15;126(49):16267-74. doi: 10.1021/ja0451970.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amiloride / analogs & derivatives
  • Amiloride / pharmacology
  • Electric Impedance
  • Human Immunodeficiency Virus Proteins
  • Ion Channels / antagonists & inhibitors
  • Ion Channels / chemistry*
  • Ion Channels / metabolism
  • Lipid Bilayers / chemistry*
  • Lipid Bilayers / metabolism
  • Membrane Potentials
  • Membranes, Artificial
  • Microscopy, Electron, Scanning
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Structure, Tertiary
  • Silicon / chemistry
  • Viral Regulatory and Accessory Proteins / antagonists & inhibitors
  • Viral Regulatory and Accessory Proteins / chemistry*
  • Viral Regulatory and Accessory Proteins / metabolism

Substances

  • Human Immunodeficiency Virus Proteins
  • Ion Channels
  • Lipid Bilayers
  • Membranes, Artificial
  • Peptide Fragments
  • Viral Regulatory and Accessory Proteins
  • vpu protein, Human immunodeficiency virus 1
  • Amiloride
  • Silicon