Self-Templated, Enantioselective Assembly of an Amyloid-like Dipeptide into Multifunctional Hierarchical Helical Arrays

Chiral self-assembly of peptides
has attracted great interest owing
to their promising applications in biomedicine, chemistry, and materials
science. However, compared with the rich knowledge about their chiral
self-assembly at the molecular or nanoscale, the formation of long-range-ordered
hierarchical helical arrays (HHAs) from simple peptides remains a
formidable challenge. Herein, we report the self-templated assembly
of an amyloid-like dipeptide into long-range-ordered HHAs by their
spontaneous fibrillization and hierarchical helical assembly within
a confined film. The chiral interactions between the peptide and diamines
result in geometry frustration and the phase transition of self-assembling
peptide films from achiral spherulite structures into chiral HHAs.
By changing the chirality and enantioselective interactions, we can
control the phase behavior, handedness, and chiroptics of the self-assembled
HHAs precisely. Moreover, the redox activity of the HHAs allows the in situ decoration of nanoparticles with high catalytic
activity. These results provide insights into the chiral self-assembly
of peptides and the fabrication of highly ordered materials with complex
architectures and promising applications in chiroptics and catalysis.