Effective stabilization of short peptide chains into a helical structure has been a challenge in the fields of chemistry and biology. Here we report a novel method for alpha-helix stabilization of short peptides through their confinement in a cyclic architecture. We synthesized block peptides based on a short peptide and a flexible linker as linear precursors. Subsequent cyclization of the peptide precursors resulted in a conformational change of the peptide unit from a random coil to an alpha-helix. The incorporation of hydrophobic residues into the peptide unit led to a facially amphiphilic conformation of the molecular cycle. The resulting amphiphilic peptide self-assembled into undulated nanofibers through the directional assembly of small oblate micelles.