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Updated: Jun 29, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 6, 2013
First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with
S K Maji1, M G Drew, A Banerjee
1Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Calcutta-700 032, India. bcab@mahendra.iacs.res.in
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.
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.
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