An amyloid-like fibril forming antiparallel supramolecular β-sheet from a synthetic tripeptide: a crystallographic signature

Single crystal X-ray diffraction studies of a terminally blocked tripeptide Boc-Leu(1)-Aib(2)-Leu(3)-OMe 1 demonstrates that it adopts a bend structure without any intramolecular hydrogen bond. Peptide 1 self-assembles to form a supramolecular antiparallel β-sheet structure by various non-covalent interactions including intermolecular hydrogen bonds in the crystal and it exhibits amyloid-like fibrillar morphology in the solid state.