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 Society126(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

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