ArticleNature chemistry2017
A monodisperse transmembrane α-helical peptide barrel.
Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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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
57 citing papers in PubMed, 121 citations in OpenAlex.
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- 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
- Article
- Mechanism-Driven Screening of Membrane-Targeting and Pore-Forming Antimicrobial Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- Droplet Contact Method (DCM) for Stable and Reproducible Lipid Bilayer Formation and its Application to Nanopore Measurements.Methods in molecular biology (Clifton, N.J.) · 2026Article
- De Novo Design of α-helical Peptide Nanopores for Single-Molecule Detection Using Helix Packing Motifs.ACS nano · 2025Article
- Bottom-up design of CaNature · 2025Article
- Fabrication of cytotoxic mirror image nanopores.Nature communications · 2025Article
- Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.The Journal of membrane biology · 2025Review
- Recent progress of artificial cells in structure design, functionality and the prospects in food biotechnology.Materials today. Bio · 2025Review
- Innovative Self-Assembly of 15-Mer Chimeric α-Peptide-Oligourea Foldamers toward ClSmall science · 2024Article
- Sculpting conducting nanopore size and shape through de novo protein design.Science (New York, N.Y.) · 2024Article
- Conformational flexibility driving charge-selective substrate translocation across a bacterial transporter.Chemical science · 2024Article
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Lipid vesicle-based molecular robots.Lab on a chip · 2024Review
- Sparks of function by de novo protein design.Nature biotechnology · 2024Review
- Article
- Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries.Journal of the American Chemical Society · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The fabrication of monodisperse transmembrane barrels formed from short synthetic peptides has not been demonstrated previously. This is in part because of the complexity of the interactions between peptides and lipids within the hydrophobic environment of a membrane. Here we report the formation of a transmembrane pore through the self-assembly of 35 amino acid α-helical peptides. The design of the peptides is based on the C-terminal D4 domain of the Escherichia coli polysaccharide transporter Wza. By using single-channel current recording, we define discrete assembly intermediates and show that the pore is most probably a helix barrel that contains eight D4 peptides arranged in parallel. We also show that the peptide pore is functional and capable of conducting ions and binding blockers. Such α-helix barrels engineered from peptides could find applications in nanopore technologies such as single-molecule sensing and nucleic-acid sequencing.
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What OpenQuestion holds
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.