ArticleNature communications2022
Assembly of transmembrane pores from mirror-image peptides.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- A self-assembled peptide forms α-helical nanopores for ultrasensitive biomarker profiling.Nature nanotechnology · 2026Article
- Large-Diameter DNA-Scaffolded Nanopores Enabled by Loosely Packed Peptides for Single-Molecule Sensing.Angewandte Chemie (International ed. in English) · 2026Article
- Interfacial Interactions of Nanoparticles and Molecular Nanostructures with Model Membrane Systems: Mechanisms, Methods, and Applications.Membranes · 2026Review
- Mechanism-Driven Screening of Membrane-Targeting and Pore-Forming Antimicrobial Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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
- Innovative Self-Assembly of 15-Mer Chimeric α-Peptide-Oligourea Foldamers toward ClSmall science · 2024Article
- Lipid vesicle-based molecular robots.Lab on a chip · 2024Review
- Electrophysiological properties and structural prediction of the SARS-CoV-2 viroprotein E.Frontiers in molecular biosciences · 2024Article
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9 authors.
Funding
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Abstract
Tailored transmembrane alpha-helical pores with desired structural and functional versatility have promising applications in nanobiotechnology. Herein, we present a transmembrane pore DpPorA, based on the natural pore PorACj, built from D-amino acid α-helical peptides. Using single-channel current recordings, we show that DpPorA peptides self-assemble into uniform cation-selective pores in lipid membranes and exhibit properties distinct from their L-amino acid counterparts. DpPorA shows resistance to protease and acts as a functional nanopore sensor to detect cyclic sugars, polypeptides, and polymers. Fluorescence imaging reveals that DpPorA forms well-defined pores in giant unilamellar vesicles facilitating the transport of hydrophilic molecules. A second D-amino acid peptide based on the polysaccharide transporter Wza forms transient pores confirming sequence specificity in stable, functional pore formation. Finally, molecular dynamics simulations reveal the specific alpha-helical packing and surface charge conformation of the D-pores consistent with experimental observations. Our findings will aid the design of sophisticated pores for single-molecule sensing related technologies.
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