Patterned Peptide Multilayer Thin Films with Nanoscale Order Through Engineered Liquid Crystallinity

Self‐assembling polypeptide molecules have been designed to explore aspects of hierarchical or multiscale long‐range order, and the interactions that occur at various length scales that drive order and patterning in complex materials. Three peptides were synthesized with repetitive motifs loosely based on insect silks. Thin films were obtained from each peptide using a solvent templating technique. Smectic layers were observed in the thin films and in bulk materials prepared for comparison. A variety of additional effects, including chirality and interfacial anchoring at the helix, compete in the thin films, resulting in complex but regular patterns within the materials over a hierarchy of length scales spanning several orders of magnitude. The relative magnitude of these effects can be tuned through sequence design, as can the smectic layer thickness. Thus, many parameters describing the patterns in the materials can be controlled at the molecular design level, allowing complex patterns of nanoscale to microscale topography and chemistry to be created through self‐assembly. In addition to the potential for designer materials, there may be some biological relevance to the observed phenomena. The silk‐like molecules used fold into “hairpins,” providing a rigid unit that can drive liquid crystalline phase behavior. A similar process could be at work in silks and other structurally similar proteins that form textured materials. Chiral smectic order and multiscale patterns that can often result are clearly rich areas, worthy of further exploration.