Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly

Semion Censor, Jorge Vega Martin, Ohad Silberbush, Samala Murali Mohan Reddy, Ran Zalk, Lonia Friedlander, Daniel G. Trabada, Jesús Mendieta, Guillaume Le Saux, Jesús Ignacio Mendieta Moreno, Linda Angela Zotti, José Ortega Mateo, Nurit Ashkenasy

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish
JournalAdvanced Materials
DOIs
StateAccepted/In press - 1 Jan 2024

Keywords

  • molecular dynamic simulations
  • peptides
  • proton channels
  • proton transport
  • self-assembly

ASJC Scopus subject areas

  • General Materials Science
  • Mechanics of Materials
  • Mechanical Engineering

Fingerprint

Dive into the research topics of 'Long-Range Proton Channels Constructed via Hierarchical Peptide Self-Assembly'. Together they form a unique fingerprint.

Cite this