Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu(1-32) from HIV-1
2004 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu(1-32) from HIV-1
Römer, W.; Lam, Y. H.; Fischer, D.; Watts, A.; Fischer, W. B.; Göring, P. & Wehrspohn, R. B. et al. (2004)
Journal of the American Chemical Society, 126(49) pp. 16267-16274. DOI: https://doi.org/10.1021/ja0451970
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- Authors
- Römer, Winfried; Lam, Yuen H.; Fischer, Daniela; Watts, Anthony; Fischer, Wolfgang B.; Göring, Petra; Wehrspohn, Ralf B.; Gösele, Ulrich; Steinem, Claudia
- 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.
- Issue Date
- 2004
- Journal
- Journal of the American Chemical Society
- ISSN
- 0002-7863
- Language
- English