Stacking interactions by two Phe side chains stabilize and orient assemblies of even the minimal amphiphilic β-sheet motifElectronic supplementary information (ESI) available: Experimental and Fig. S1-S9. See DOI: 10.1039/c4cc09673h

Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions. Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions.