Determination of regions involved in amyloid fibril formation for Aβ(1-40) peptide
| Autor: | Oxana V. Galzitskaya, M. Yu. Suvorina, Elizaveta I. Grigorashvili, Olga M. Selivanova, Alexey K. Surin |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Spectrometry Mass Electrospray Ionization Proteases Protein Conformation Peptide Crystallography X-Ray Tandem mass spectrometry Biochemistry 03 medical and health sciences 0302 clinical medicine Bioorganic chemistry Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Chromatography High Pressure Liquid chemistry.chemical_classification Amyloid beta-Peptides P3 peptide General Medicine Amyloid fibril Peptide Fragments Biochemistry of Alzheimer's disease Microscopy Electron 030104 developmental biology chemistry Proteolysis 030217 neurology & neurosurgery |
| Zdroj: | Biochemistry (Moscow). 81:762-769 |
| ISSN: | 1608-3040 0006-2979 |
| Popis: | The studies of amyloid structures and the process of their formation are important problems of biophysics. One of the aspects of such studies is to determine the amyloidogenic regions of a protein chain that form the core of an amyloid fibril. We have theoretically predicted the amyloidogenic regions of the Aβ(1-40) peptide capable of forming an amyloid structure. These regions are from 16 to 21 and from 32 to 36 amino acid residues. In this work, we have attempted to identify these sites experimentally by the method of tandem mass spectrometry. As a result, we show that regions of the Aβ(1-40) peptide from 16 to 22 and from 28 to 40 amino acid residues are resistant to proteases, i.e. they are included in the core of amyloid fibrils. Our results correlate with the results of the theoretical prediction. |
| Databáze: | OpenAIRE |
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