Transmembrane peptide NB of influenza B: A simulation, structure, and conductance study

W. B. Fischer*, M. Pitkeathly, B. A. Wallace, L. R. Forrest, G. R. Smith, M. S.P. Sansom

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


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 α-helical-like structure. Computational models of α-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.

Original languageEnglish
Pages (from-to)12708-12716
Number of pages9
Issue number41
StatePublished - 17 Oct 2000


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