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

doi:10.1021/ja0451970

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^*

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生醫光電研究所

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摘要

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 Vpu_1-32, which forms helix bundles with characteristic opening states. We elucidated different amilorides as potential drugs to inhibit channel activity of Vpu.

原文	English
頁（從 - 到）	16267-16274
頁數	8
期刊	Journal of the American Chemical Society
卷	126
發行號	49
DOIs	https://doi.org/10.1021/ja0451970
出版狀態	Published - 15 12月 2004

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

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 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.",

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AU - Römer, Winfried

AU - Lam, Yuen H.

AU - Fischer, Dahlia

AU - Watts, Anthony

AU - Fischer, Wolfgang B.

AU - Göring, Petra

AU - Wehrspohn, Ralf B.

AU - Gösele, Ulrich

AU - Steinem, Claudia

PY - 2004/12/15

Y1 - 2004/12/15

N2 - 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.

AB - 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.

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

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Channel activity of a viral transmembrane peptide in micro-BLMs: Vpu _1-32 from HIV-1