Morphology control of one-dimensional peptide nanostructures.

Self-assembly of peptides has gathered particular attentions since it may provide unique properties relying on highly specific molecular recognition and structural organization. Peptides assemble into complex nanostructures through highly specific biomolecular interactions such as hydrogen bonding and hydrophobic interaction. Among various nanostructured materials, one-dimensional nanostructures, such as nanowires, nanotubes, and nanoribbons, have been intensively investigated. However, so far, systematic investigations on the morphological variation of peptide-assembly have rarely been explored. Here we demonstrate the morphological diversity of the self-assembly of an aromatic peptide unit. The aromatic dipeptides spontaneously assembled into nanotubes, nanoribbons, and nanowires in various polar solvents. Our work provides a broad spectrum of one-dimensional nanostructured materials, which are potentially significant for nanofabrication.