Self-assembly of FRV3 FR peptide into supramolecular nanofibrils

Small peptides are commonly used monomers for the self -assembly of biologically relevant supramolecular nanomaterials. In this study, the heptameric sequence FRV 3 FR was found to self -assemble into nanofibrils in solution, as confirmed by transmission electron microscopy (TEM), leading to the subsequent formation of hydrogels. Circular dichroism (CD) analysis showed that the FRV 3 FR peptide adopts a secondary structure that closely resembles a beta-turn type conformation. An alanine-based peptide termed FRA 3 FR was also studied to highlight the impact of the middle amino acid triad has in self -assembly. Even though the FRA 3 FR showed a similar CD signal, it failed to provide any significant nanostructure or hydrogel formation, demonstrating the ability valine residues over alanine in promoting self -assembly. This work presents preliminary studies on a novel peptide sequence, laying the groundwork for its potential development into a functional peptide -based nanomaterial.