ArticleBiophysical journal2002
Modifications of alamethicin ion channels by substitution of Glu-7 for Gln-7.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- Multi-oligomeric states of alamethicin ion channel: Assemblies and conductance.Biophysical journal · 2023Article
- Validity of the Electrodiffusion Model for Calculating Conductance of Simple Ion Channels.The journal of physical chemistry. B · 2017Article
- Alamethicin Supramolecular Organization in Lipid Membranes fromBiophysical journal · 2016Article
- A thermodynamic approach to alamethicin pore formation.Biochimica et biophysica acta · 2014Article
- The pH-dependent induction of lipid membrane ionic permeability by N-terminally lysine-substituted analogs of gramicidin A.European biophysics journal : EBJ · 2012Article
- Metal-assisted channel stabilization: disposition of a single histidine on the N-terminus of alamethicin yields channels with extraordinarily long lifetimes.Biophysical journal · 2010Article
- Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin.European biophysics journal : EBJ · 2004Review
- Ion channels of alamethicin dimer N-terminally linked by disulfide bond.Biophysical journal · 2003Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To evaluate the role of charged residues facing a pore lumen in stability of channel structure and ion permeation, we studied electrical properties of ion channels formed by synthesized native alamethicins (Rf50 (alm-Q7Q18) and Rf30 (alm-Q7E18)) and their analogs with Glu-7 (alm-E7Q18 and alm-E7E18). The single-channel currents were measured over a pH range of 3.5 to 8.7 using planar bilayers of diphytanoyl PC. The peptides all showed multi-level current fluctuations in this pH range. At pH 3.5 the channels formed by the four peptides were similar to each other irrespective of the side chain differences at positions 7 and 18. The ionization of Glu-7 (E7) and Glu-18 (E18) above neutral pH reduced the relative probabilities of low-conductance states (levels 1 and 2) and increased those of high-conductance states (levels 4-6). The channel conductance of the peptides with E7 and/or E18, which was distinct from that of alm-Q7Q18, showed a marked pH-dependence, especially for low-conductance states. The ionization of E7 further reduced the stability of channel structure, altered the current-voltage curve from a superlinear relation to a sublinear one, and enhanced cation selectivity. These results indicate that ionized E7 strongly influences the channel structure and the ion permeation, in contrast to ionized E18.
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