Constitutionally Isomeric Aromatic Tripeptides: Self-Assembly and Metal-Ion-Modulated Transformations

Self-assembling peptides based on aromatic amino acids can adopt diverse nanostructures which primarily depend on their molecular structures. Therefore, to understand the nature of self-assembly on the molecular level we rationally designed two constitutional isomers of short aromatic peptides. The first isomer consists of a tyrosine moiety at the N-terminus and the second isomer consists of a tyrosine moiety at the C-terminus of the FF peptide, a core recognition motif of Amyloid β peptides. Therefore, it can be considered that both the designed tripeptides are the analogues of the FFF peptide with only atomic(-H) level replacement by -OH functional group on the first and last phenyl ring, respectively. The first isomer self-assembled into 2D porous nanosheets ("Nanowebs"), however the second isomers produced toroidal shapes with central spheres ("Nano-Saturn" like assemblies). Interestingly, the presence of the transition-metal ions (copper, zinc and iron) triggered the self-assembly of both the peptides into fibrous circular discs, nanomats and nanoplates like assembly.