Self-assembly of a tetrapeptide in which a unique supramolecular helical structure is formed via intermolecular hydrogen bonding in the solid state

A single crystal X-ray diffraction study of the tetrapeptide Boc-Ala1-Aib2-Leu3-Aib4-OMe 1 (Aib: α-aminoisobutyric acid) reveals that it forms a supramolecular helix through continuous intermolecular hydrogen bonds. Scanning electron microscopic studies show that this peptide exhibits amyloid-like fibrillar morphology in the solid state.