Many
peptides are able to self-assemble into one-dimensional (1D)
nanostructures, such as cylindrical fibers or ribbons of variable
widths, but the relationship between the morphology of 1D objects
and their molecular structure is not well understood. Here, we use
coarse-grained molecular dynamics (CG-MD) simulations to study the
nanostructures formed by self-assembly of different peptide amphiphiles
(PAs). The results show that ribbons are hierarchical superstructures
formed by laterally assembled cylindrical fibers. Simulations starting
from bilayer structures demonstrate the formation of filaments, whereas
other simulations starting from filaments indicate varying degrees
of interaction among them depending on chemical structure. These interactions
are verified by observations using atomic force microscopy of the
various systems. The interfilament interactions are predicted to be
strongest in supramolecular assemblies that display hydrophilic groups
on their surfaces, while those with hydrophobic ones are predicted
to interact more weakly as confirmed by viscosity measurements. The
simulations also suggest that peptide amphiphiles with hydrophobic
termini bend to reduce their interfacial energy with water, which
may explain why these systems do not collapse into superstructures
of bundled filaments. The simulations suggest that future experiments
will need to address mechanistic questions about the self-assembly
of these systems into hierarchical structures, namely, the preformation
of interactive filaments vs equilibration of large assemblies into
superstructures.