Peptide-Carbon Nanotube Hybrids under Confinement: Structure and Stability from Atomistic Simulations
Karinna Mendanha1, Guilherme Colherinhas1
1Instituto de Física, Universidade Federal de Goiás, Goiânia 74690-900, GO, Brazil.
ACS Omega
|March 2, 2026
Summary
Peptides confined in carbon nanotubes (CNTs) remain flexible due to water interactions, not aggregation. This peptide-CNT interaction is key for bioelectronic interfaces and nanocarriers.
Area of Science:
- Nanomaterials Science
- Biophysics
- Computational Chemistry
Background:
- Biofunctional nanomaterials combining flexibility and electronic properties are crucial for advanced applications.
- Understanding peptide-carbon nanotube (CNT) interactions is key to designing these materials.
Purpose of the Study:
- To investigate the structural and energetic behavior of A6D peptides confined within a single-walled CNT.
- To elucidate the role of intermolecular forces and solvent interactions in peptide organization under confinement.
Main Methods:
- Classical molecular dynamics simulations were employed to model the A6D peptide system within a CNT.
- Analysis included hydrogen-bond dynamics, electrostatic and van der Waals energies, and Ramachandran distributions.
Main Results:
- Peptide-solvent interactions dominated over peptide-peptide aggregation, maintaining high peptide flexibility.
- Alanine residues showed hydrophobic attraction to the CNT, while aspartic acid residues interacted with water.
- Confined peptides adopted stable alpha-helical structures, forming a peptide-membrane-like internal structure.
Conclusions:
- Electrostatic and dispersion forces, alongside solvent effects, govern peptide organization and stability within CNTs.
- The findings support the potential of peptide-coated CNTs for bioelectronic interfaces, molecular transport, and drug delivery systems.
