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

Roemer, Winfried and Lam, Y. H. and Fischer, D. and Watts, A. and Fischer, Wolfgang B. and Goering, P. and Wehrspohn, R. B. and Goesele, U. and Steinem, Claudia (2004) Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu(1-32) from HIV-1. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 126 (49). pp. 16267-16274. ISSN 0002-7863,

Full text not available from this repository. (Request a copy)

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 muF/cm(2). Membrane resistances were in the GOmega-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.

Item Type: Article
Uncontrolled Keywords: IMMUNODEFICIENCY-VIRUS TYPE-1; LIPID BILAYER-MEMBRANES; ION CHANNELS; PROTEIN VPU; MICROMACHINED SUPPORTS; PHOSPHOLIPID-BILAYERS; COMPUTER-SIMULATIONS; IMPEDANCE ANALYSIS; FULL-LENGTH; SILICON;
Subjects: 500 Science > 540 Chemistry & allied sciences
Divisions: Chemistry and Pharmacy > Institut für Analytische Chemie, Chemo- und Biosensorik
Depositing User: Dr. Gernot Deinzer
Date Deposited: 21 Jun 2021 08:29
Last Modified: 21 Jun 2021 08:29
URI: https://pred.uni-regensburg.de/id/eprint/36867

Actions (login required)

View Item View Item