Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study.
The putative transmembrane segment of the ion channel forming peptide NB from influenza B was synthesized by standard solid-phase peptide synthesis. Insertion into the planar lipid bilayer revealed ion channel activity with conductance levels of 20, 61, 107, and 142 pS in a 0.5 M KCl buffer solution...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2000
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| _version_ | 1797105940334379008 |
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| author | Fischer, W Pitkeathly, M Wallace, B Forrest, L Smith, G Sansom, MS |
| author_facet | Fischer, W Pitkeathly, M Wallace, B Forrest, L Smith, G Sansom, MS |
| author_sort | Fischer, W |
| collection | OXFORD |
| description | The putative transmembrane segment of the ion channel forming peptide NB from influenza B was synthesized by standard solid-phase peptide synthesis. Insertion into the planar lipid bilayer revealed ion channel activity with conductance levels of 20, 61, 107, and 142 pS in a 0.5 M KCl buffer solution. In addition, levels at -100 mV show conductances of 251 and 413 pS. A linear current-voltage relation reveals a voltage-independent channel formation. In methanol and in vesicles the peptide appears to adopt an alpha-helical-like structure. Computational models of alpha-helix bundles using N = 4, 5, and 6 NB peptides per bundle revealed water-filled pores after 1 ns of MD simulation in a solvated lipid bilayer. Calculated conductance values [using HOLE (Smart et al. (1997) Biophys. J. 72, 1109-1126)] of ca. 20, 60, and 90 pS, respectively, suggested that the multiple conductance levels seen experimentally must correspond to different degrees of oligomerization of the peptide to form channels. |
| first_indexed | 2024-03-07T06:54:33Z |
| format | Journal article |
| id | oxford-uuid:fdb11b1f-1545-4ba9-aaad-26b7a1b3f152 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:54:33Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:fdb11b1f-1545-4ba9-aaad-26b7a1b3f1522022-03-27T13:30:43ZTransmembrane peptide NB of influenza B: a simulation, structure, and conductance study.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fdb11b1f-1545-4ba9-aaad-26b7a1b3f152EnglishSymplectic Elements at Oxford2000Fischer, WPitkeathly, MWallace, BForrest, LSmith, GSansom, MSThe putative transmembrane segment of the ion channel forming peptide NB from influenza B was synthesized by standard solid-phase peptide synthesis. Insertion into the planar lipid bilayer revealed ion channel activity with conductance levels of 20, 61, 107, and 142 pS in a 0.5 M KCl buffer solution. In addition, levels at -100 mV show conductances of 251 and 413 pS. A linear current-voltage relation reveals a voltage-independent channel formation. In methanol and in vesicles the peptide appears to adopt an alpha-helical-like structure. Computational models of alpha-helix bundles using N = 4, 5, and 6 NB peptides per bundle revealed water-filled pores after 1 ns of MD simulation in a solvated lipid bilayer. Calculated conductance values [using HOLE (Smart et al. (1997) Biophys. J. 72, 1109-1126)] of ca. 20, 60, and 90 pS, respectively, suggested that the multiple conductance levels seen experimentally must correspond to different degrees of oligomerization of the peptide to form channels. |
| spellingShingle | Fischer, W Pitkeathly, M Wallace, B Forrest, L Smith, G Sansom, MS Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title | Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title_full | Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title_fullStr | Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title_full_unstemmed | Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title_short | Transmembrane peptide NB of influenza B: a simulation, structure, and conductance study. |
| title_sort | transmembrane peptide nb of influenza b a simulation structure and conductance study |
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