First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids.
The model tripeptide Boc-beta-Ala(1)-Aib(2)-beta-Ala(3)-OMe 1 [beta-Ala: beta-alanine, Aib: alpha-aminoisobutyric acid] forms an infinite parallel beta-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.
Maji
S K
SK
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Calcutta-700 032, India. bcab@mahendra.iacs.res.in
Drew
M G
MG
Banerjee
A
A
D000596:Amino Acids / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000596:Amino Acids; D016229:Amyloid beta-Peptides; D009842:Oligopeptides