First crystallographic signature of amyloid-like fibril forming β-sheet assemblage from a tripeptide with non-coded amino acids

Abstract

The model tripeptide Boc-β-Ala(1)-Aib(2)-β-Ala(3)-OMe 1 [β-Ala: β-alanine, Aib: α-aminoisobutyric acid] forms an infinite parallel β-sheet structure through intermolecular interactions in single crystals and from the SEM diagram of this peptide, it is evident that the compound has fibrillar morphology, a characteristic of neurodegenerative disease causing amyloid aggregate.