Unraveling the influence of aromatic endcaps in peptide self-assembly

Aromatic peptides are an emerging class of building units for molecular self-assembly and creation of functional biomaterials. The strength of aromatic association plays an essential role in the self-assembly of aromatic peptides. Here, we design a series of aromatic peptides with different hydrophobic domains but the same peptide sequence. The hydrophobicity and aromaticity can be carefully regulated by the number of benzene rings and the alkyl spacer between the benzene and peptide regions. Upon the continuous enhancement of aromaticity, diverse supramolecular nanostructures, including nanotubes, nanofibers, and short helical ribbons, were clearly observed. The peptide with diphenyl groups exhibits the highest regularity of molecular packing, due to the synergy of force balance between hydrogen bonding and π–π interactions. In addition, the incorporation of a spacer in between the aromatic and peptide regions facilitates the self-assembly capability, as the interference between aromatic association and hydrogen bonding is hindered. These dramatic results demonstrate that aromaticity serves as an effective and robust parameter in the molecular arrangement, providing a new perspective into the formation and evolution of supramolecular assembly.