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

Area of Science:

• Biomimetic chemistry
• Nanotechnology
• Supramolecular chemistry

Background:

• Natural proton channels are crucial for biological energy processes.
• Mimicking these channels with artificial systems is a key challenge in nanotechnology.
• Peptide self-assembly offers a promising route to create ordered nanostructures.

Purpose of the Study:

• To design and fabricate peptide-based artificial nanochannels for efficient proton transport.
• To investigate the self-assembly mechanism and structural properties of these peptide channels.
• To evaluate the proton transport efficiency and compare it with natural systems.

Main Methods:

• Hierarchical self-assembly of cyclic peptides into micrometers-long nanotubes.
• Utilizing intermolecular aromatic interactions for nanotube alignment.
• Incorporating titratable amino acid sidechains and counter ions within the nanochannels.

Main Results:

• Successfully formed micrometers-long proton nanochannels via hierarchical peptide self-assembly.
• Demonstrated efficient proton transport through hydrogen-bonded chains within the channels.
• Achieved proton transfer rates comparable to natural protein channels over micrometer distances.
• Enhanced proton flow density and rate through interaction with counter ions.

Conclusions:

• Hierarchical peptide self-assembly provides a viable strategy for creating functional proton nanochannels.
• These artificial channels exhibit biomimetic proton transport capabilities.
• The recyclable and biocompatible nature of these systems suggests broad applicability in energy, medicine, and electronics.