Long-range proton channels constructed via hierarchical peptide self-assembly

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 micromet...

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Autores: Censor, Semion, Vega Martín, Jorge, Silberbush, Ohad, Reddy, Samala Murali Mohan, Zalk, Ran, Friedlander, Lonia, Trabada, Daniel G., Mendieta, Jesús, Le Saux, Guillaume, Moreno, Jesús Ignacio Mendieta, Zotti, Linda Ángela, Ortega Mateo, José, Ashkenasy, Nurit
Formato: artículo
Fecha de publicación:2024
País:España
Recursos:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/719057
Acesso em linha:http://hdl.handle.net/10486/719057
https://dx.doi.org/10.1002/adma.202409248
Access Level:acceso abierto
Palavra-chave:molecular dynamic simulations
peptides
proton channels
proton transport
self-assembly
Física
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spelling Long-range proton channels constructed via hierarchical peptide self-assemblyCensor, SemionVega Martín, JorgeSilberbush, OhadReddy, Samala Murali MohanZalk, RanFriedlander, LoniaTrabada, Daniel G.Mendieta, JesúsLe Saux, GuillaumeMoreno, Jesús Ignacio MendietaZotti, Linda ÁngelaOrtega Mateo, JoséAshkenasy, Nuritmolecular dynamic simulationspeptidesproton channelsproton transportself-assemblyFísicaThe 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 bioelectronicsThe authors acknowledge the financial support of the Spanish Ministry of Science and Innovation through project no. PID2021\u2010125604NB, and through the \u201CMar\u00EDa de Maeztu\u201D Programme for Units of Excellence in R&D (CEX2023\u2010001316\u2010M).WileyDepartamento de Física Teórica de la Materia CondensadaFacultad de Ciencias20242024-12-12research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/719057https://dx.doi.org/10.1002/adma.202409248reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/7190572026-06-23T12:46:27Z
dc.title.none.fl_str_mv Long-range proton channels constructed via hierarchical peptide self-assembly
title Long-range proton channels constructed via hierarchical peptide self-assembly
spellingShingle Long-range proton channels constructed via hierarchical peptide self-assembly
Censor, Semion
molecular dynamic simulations
peptides
proton channels
proton transport
self-assembly
Física
title_short Long-range proton channels constructed via hierarchical peptide self-assembly
title_full Long-range proton channels constructed via hierarchical peptide self-assembly
title_fullStr Long-range proton channels constructed via hierarchical peptide self-assembly
title_full_unstemmed Long-range proton channels constructed via hierarchical peptide self-assembly
title_sort Long-range proton channels constructed via hierarchical peptide self-assembly
dc.creator.none.fl_str_mv Censor, Semion
Vega Martín, Jorge
Silberbush, Ohad
Reddy, Samala Murali Mohan
Zalk, Ran
Friedlander, Lonia
Trabada, Daniel G.
Mendieta, Jesús
Le Saux, Guillaume
Moreno, Jesús Ignacio Mendieta
Zotti, Linda Ángela
Ortega Mateo, José
Ashkenasy, Nurit
author Censor, Semion
author_facet Censor, Semion
Vega Martín, Jorge
Silberbush, Ohad
Reddy, Samala Murali Mohan
Zalk, Ran
Friedlander, Lonia
Trabada, Daniel G.
Mendieta, Jesús
Le Saux, Guillaume
Moreno, Jesús Ignacio Mendieta
Zotti, Linda Ángela
Ortega Mateo, José
Ashkenasy, Nurit
author_role author
author2 Vega Martín, Jorge
Silberbush, Ohad
Reddy, Samala Murali Mohan
Zalk, Ran
Friedlander, Lonia
Trabada, Daniel G.
Mendieta, Jesús
Le Saux, Guillaume
Moreno, Jesús Ignacio Mendieta
Zotti, Linda Ángela
Ortega Mateo, José
Ashkenasy, Nurit
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Física Teórica de la Materia Condensada
Facultad de Ciencias
dc.subject.none.fl_str_mv molecular dynamic simulations
peptides
proton channels
proton transport
self-assembly
Física
topic molecular dynamic simulations
peptides
proton channels
proton transport
self-assembly
Física
description 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
publishDate 2024
dc.date.none.fl_str_mv 2024
2024-12-12
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/719057
https://dx.doi.org/10.1002/adma.202409248
url http://hdl.handle.net/10486/719057
https://dx.doi.org/10.1002/adma.202409248
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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