ArticleBiophysical journal2003
Ion channels of alamethicin dimer N-terminally linked by disulfide bond.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Computational design of antimicrobial peptide nanopores.Nature chemical biology · 2026Article
- Large-Diameter DNA-Scaffolded Nanopores Enabled by Loosely Packed Peptides for Single-Molecule Sensing.Angewandte Chemie (International ed. in English) · 2026Article
- Multi-oligomeric states of alamethicin ion channel: Assemblies and conductance.Biophysical journal · 2023Article
- Heterosynaptic plasticity in biomembrane memristors controlled by pH.MRS bulletin · 2023Article
- Effect of Cobalt Ferrite Nanoparticles in a Hydrophilic Shell on the Conductance of Bilayer Lipid Membrane.Membranes · 2022Article
- Structure and water permeability of fully hydrated diphytanoylPC.Chemistry and physics of lipids · 2010Article
- Metal-assisted channel stabilization: disposition of a single histidine on the N-terminus of alamethicin yields channels with extraordinarily long lifetimes.Biophysical journal · 2010Article
- Peptide aggregation and pore formation in a lipid bilayer: a combined coarse-grained and all atom molecular dynamics study.Biophysical journal · 2008Article
- Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin.European biophysics journal : EBJ · 2004Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A covalent dimer of alamethicin Rf30 was synthesized by linking the N-termini by a disulfide bond. When the dimer peptides were added to the cis-side of a diphytanoyl PC membrane, macroscopic channel current was induced only at cis positive voltages. The single-channel recordings showed several conductance levels that were alternately stabilized. These results indicate that the dimer peptides form stable channels by N-terminal insertion like alamethicin and that most of the pores are assembled from even numbers of helices. Taking advantages of the long open duration of the dimer peptide channels, the current-voltage (I-V) relations of the single-channels were obtained by applying fast voltage ramps during the open states. The I-V relations showed rectification, such that current from the cis-side toward the trans-side is larger than that in the opposite direction. The intrinsic rectification is mainly attributed to the macro dipoles of parallel peptide helices surrounding a central pore.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.