Long‐Range Proton Channels Constructed via Hierarchical Peptide Self‐Assembly
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.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Long‐Range Proton Channels Constructed via Hierarchical Peptide Self‐Assembly ; day:12 ; month:11 ; year:2024 ; extent:12
Advanced materials ; (12.11.2024) (gesamt 12)
- Creator
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Censor, Semion
Martin, Jorge Vega
Silberbush, Ohad
Reddy, Samala Murali Mohan
Zalk, Ran
Friedlander, Lonia
Trabada, Daniel G.
Mendieta, Jesús
Le Saux, Guillaume
Moreno, Jesús Ignacio Mendieta
Zotti, Linda Angela
Mateo, José Ortega
Ashkenasy, Nurit
- DOI
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10.1002/adma.202409248
- URN
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urn:nbn:de:101:1-2411131311579.053359028553
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:26 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Censor, Semion
- Martin, Jorge Vega
- Silberbush, Ohad
- Reddy, Samala Murali Mohan
- Zalk, Ran
- Friedlander, Lonia
- Trabada, Daniel G.
- Mendieta, Jesús
- Le Saux, Guillaume
- Moreno, Jesús Ignacio Mendieta
- Zotti, Linda Angela
- Mateo, José Ortega
- Ashkenasy, Nurit
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Controllable hierarchical self-assembly of porphyrin-derived supra-amphiphiles
Hierarchical self-assembly of 3D lattices from polydisperse anisometric colloids
Hierarchical Superstructures by Combining Crystallization‐Driven and Molecular Self‐Assembly
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Bioinspired enzymatic compartments constructed by spatiotemporally confined in situ self-assembly of catalytic peptide
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Controllable hierarchical self-assembly of porphyrin-derived supra-amphiphiles
Hierarchical self-assembly of 3D lattices from polydisperse anisometric colloids
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