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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.

Type

Journal article

Journal

Biochemistry

Publication Date

17/10/2000

Volume

39

Pages

12708 - 12716

Keywords

Amino Acid Sequence, Circular Dichroism, Computer Simulation, Electric Conductivity, Electric Stimulation, Influenza B virus, Ion Channels, Lipid Bilayers, Membrane Glycoproteins, Models, Biological, Models, Chemical, Models, Molecular, Molecular Sequence Data, Peptides, Protein Structure, Secondary, Software, Structure-Activity Relationship, Viral Proteins, Water