Peptide Aβ(16-25) forms nanofilms in the process of its aggregation
| Autor: | M. Yu. Suvorina, Elizaveta I. Grigorashvili, E. Yu. Gorbunova, Leila G. Mustaeva, Olga M. Selivanova, Oxana V. Galzitskaya, Alexey K. Surin |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Spectrometry Mass Electrospray Ionization 030106 microbiology Peptide Crystallography X-Ray Biochemistry Oligomer Protein Structure Secondary law.invention Nanomaterials 03 medical and health sciences chemistry.chemical_compound law Bioorganic chemistry chemistry.chemical_classification Amyloid beta-Peptides P3 peptide General Medicine Amyloid fibril Nanostructures Microscopy Electron Crystallography 030104 developmental biology chemistry Polymerization Electron microscope |
| Zdroj: | Biochemistry (Moscow). 81:755-761 |
| ISSN: | 1608-3040 0006-2979 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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