Peptide Aβ(16-25) forms nanofilms in the process of its aggregation

• Published in: Biochemistry (Moscow) Vol. 81; no. 7; pp. 755 - 761
• Main Authors: Selivanova, O. M., Gorbunova, E. Yu, Mustaeva, L. G., Grigorashvili, E. I., Suvorina, M. Yu, Surin, A. K., Galzitskaya, O. V.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.07.2016
• Subjects: Amyloid - chemistry; Amyloid - metabolism; Amyloid beta-Peptides - metabolism; Biochemistry; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Crystallography, X-Ray; Life Sciences; Microbiology; Microscopy, Electron; Nanostructures - chemistry; Protein Structure, Secondary; Spectrometry, Mass, Electrospray Ionization; protofibril; oligomer; electron microscopy; Aβ peptide; amyloid fibril; Alzheimer’s disease
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297916070129

A method for the synthesis and high purification of fragments of Aβ(1-42) peptide has been elaborated. We have synthesized the amyloidogenic fragment Aβ(16-25) predicted by us and studied the process of its aggregation by electron microscopy and X-ray analysis. Electron microscopy images show that the peptide forms a film, which is not characteristic of amyloid fibrils. At the same time, according to the X-ray diffraction data, its preparations display the presence of two main reflections (4.6-4.8 and 8-12 Å) characteristic of cross-β structure of amyloid fibrils. Thus, the fragment Aβ(16-25) that we predicted is a promising object not only for studying the process of polymerization of the peptides/proteins, but also for using it as a nanomaterial to study a number of biological processes.