Di-phenylalanine (FF), with the structure L-Phe-L-Phe, is a peptide building block associated with the pathogenesis of Alzheimer’s disease. It was identified from Alzheimer’s ␤-amyloid polypeptide studies, where it was proposed as the core recognition motif able to guide self-assembly [22]. Since Reches et al. reported that di-phenylalanine produces nanotubes [23], many studies have been carried out to form a variety of functional nanostructures from FF-based build- ing blocks such as nanotubes, spherical vesicles, nanofibrils, nanowires, and ordered molecular chains (Fig. 2). The application of FFs includes bioimaging, biosensors, guest encapsulation, nanofabrication as well as drug delivery. FF is an aromatic dipeptide that displays interesting features as a building block for tubular nanostructures. In its self-assembly, cyclic hexamers are formed with six FF units (Fig. 3). Subsequently, stacking of hexamers produces narrow channels, which leads to the forma- tion of self-assembled sheets due to hexagonal packing. The coiling of the sheets produces nanoscale tubes with hydrophobic external walls. Finally, these nanotubes can be self-assembled on even larger scales, forming bundles. The self-assembly processes are illustrated in Fig. 3. The backbone hydrogen bonds and bond interactions from the aromatic peptide side-chains hold the self-assembled FF structures together. The interactions between the side- chain aromatic rings create well-ordered tubular structures of significant length (100 m)