ArticleAdvanced materials (Deerfield Beach, Fla.)2024
Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly.
Article in Advanced materials (Deerfield Beach, Fla.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Engineered Protein-Based Ionic Conductors for Sustainable Energy Storage Applications.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Mixed Ionic and Electronic Charge Transport in Conductive Protein Fibers Revealed with DC Electrical Measurements.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Coupling between electrons' spin and proton transfer in chiral biological crystals.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Lipid polymorphism of plant thylakoid membranes. The dynamic exchange model - facts and hypotheses.Physiologia plantarumReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors.
Funding
Abstract
The quest to understand and mimic proton translocation mechanisms in natural channels has driven the development of peptide-based artificial channels facilitating efficient proton transport across nanometric membranes. It is demonstrated here that hierarchical peptide self-assembly can form micrometers-long proton nanochannels. The fourfold symmetrical peptide design leverages intermolecular aromatic interactions to align self-assembled cyclic peptide nanotubes, creating hydrophilic nanochannels between them. Titratable amino acid sidechains are positioned adjacent to each other within the channels, enabling the formation of hydrogen-bonded chains upon hydration, and facilitating efficient proton transport. Moreover, these chains are enriched with protons and water molecules by interacting with immobile counter ions introduced into the channels, increasing proton flow density and rate. This system maintains proton transfer rates closely resembling those in natural protein channels over micrometer distances. The functional behavior of these inherently recyclable and biocompatible systems opens the door for their exploitation in diverse applications in energy storage and conversion, biomedicine, and bioelectronics.
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Registered trials
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