| Many potential applications have been proposed for carbon nanotubes, yet their practical usages are limited by their extreme hydrophobicity. Dieckmann et al. designed an alpha-helical peptide, named nano-1 , to disperse single-walled carbon nanotubes (SWNTs) in aqueous solution. However, most of the detailed experimental characterization has been performed on dried samples, leaving many unanswered questions about the molecular interactions in the aqueous peptide -- SWNT complexes. Here, we used molecular dynamics simulations to study the peptide conformation at the water/SWNT interface using three different force fields. We found that the alpha-helical conformation of nano-1 is especially stable at the water/SWNT interface where it forms as many hydrogen bonds with water molecules as in pure water. In addition, nano-1 can interact with adjacent peptides on the SWNT surface without compromising the peptide -- SWNT interactions. Understanding the molecular details of the peptide -- SWNT interactions will assist future peptide design efforts. |
