We had recently demonstrated that the diphenylalanine peptide, the core recognition motif of the Alzheimer's β-amyloid polypeptide, self-assembles into a novel class of peptide nanotubes. The formation of well-ordered supramolecular structures at the nanoscale by such a simple peptide was consistent with our suggestion that aromatic interactions may provide order and directionality needed for the formation of fibrillar peptide structures. Yet, we could not rule out a contribution of the charged amine and carboxyl moieties at the termini of the short peptide. In order to explore the potential role of electrostatic interaction in the assembly process we have studied a modified non-charged peptide analogue, Ac-Phe-Phe-NH2, in which the N-terminal amine was acetylated and the C-terminal carboxyl was amidated. Scanning and transmission electron microscopy analyses demonstrated that this peptide analogue self-assembles into highly-ordered tubular structures, as observed with the NH2-Phe-Phe-COOH. Also, infrared spectroscopy revealed an amide I absorbance pattern that is very similar to that of the non-modified peptide. Furthermore, an amidated NH2-Phe-Phe-NH2 peptide, which has a net positive charge, also self-assembled into ordered tubular structures. On the other hand, the amine-modified analogues Boc-Phe-Phe-COOH, Z-Phe-Phe-COOH, and Fmoc-Phe-Phe-COOH peptides formed amyloid-like structures that had a significantly smaller diameter. Taken together, the current study further supports our hypothesis regarding the role of aromatic interactions in the self-assembly of amyloid fibrils and amyloid-associated nanostructures that can be modulated by simple chemical modifications.