Peptide A[beta] Forms Nanofilms in the Process of Its Aggregation

Peptide A[beta] Forms Nanofilms in the Process of Its Aggregation

A method for the synthesis and high purification of fragments of A[beta](1-42) peptide has been elaborated. We have synthesized the amyloidogenic fragment A[beta](16-25) predicted by us and studied the process of its aggregation by electron microscopy and X-ray analysis. Electron microscopy images s...

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Bibliographic Details
Published in:Biochemistry (Moscow) Vol. 81; no. 7; p. 755
Main Authors: Selivanova, O.M, Gorbunova, E. Yu, Mustaeva, L.G, Grigorashvili, E.I, Suvorina, M. Yu, Surin, A.K, Galzitskay, O.V
Format: Journal Article
Language:English
Published: New York Springer 01-07-2016
Springer Nature B.V
Subjects:
Electron microscopy
Peptides
X-ray diffraction
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Summary:A method for the synthesis and high purification of fragments of A[beta](1-42) peptide has been elaborated. We have synthesized the amyloidogenic fragment A[beta](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 [Angstrom]) characteristic of cross-[beta] structure of amyloid fibrils. Thus, the fragment A[beta](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. DOI: 10.1134/S0006297916070129 Key words: amyloid fibril, protofibril, oligomer, A[beta] peptide, Alzheimer's disease, electron microscopy
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297916070129