Determination of size of folding nuclei of fibrils formed from recombinant Aβ(1-40) peptide
| Autor: | Oxana V. Galzitskaya, Elizaveta I. Grigorashvili, Alexey K. Surin, Victor V. Marchenkov, Nikita V. Dovidchenko, Ulyana F. Dzhus, Olga M. Selivanova, M. Yu. Suvorina, A. O. Mikhailina |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid Spectrometry Mass Electrospray Ionization Peptide Fibril Biochemistry Oligomer Fluorescence spectroscopy law.invention 03 medical and health sciences chemistry.chemical_compound law medicine chemistry.chemical_classification Amyloid beta-Peptides 030102 biochemistry & molecular biology General Medicine Peptide Fragments Recombinant Proteins Kinetics Microscopy Electron Crystallography Spectrometry Fluorescence 030104 developmental biology Monomer medicine.anatomical_structure chemistry Recombinant DNA Electron microscope Nucleus |
| Zdroj: | Biochemistry (Moscow). 81:538-547 |
| ISSN: | 1608-3040 0006-2979 |
| Popis: | We have developed a highly efficient method for purification of the recombinant product Aβ(1-40) peptide. The concentration dependence of amyloid formation by recombinant Aβ(1-40) peptide was studied using fluorescence spectroscopy and electron microscopy. We found that the process of amyloid formation is preceded by lag time, which indicates that the process is nucleation-dependent. Further exponential growth of amyloid fibrils is followed by branching scenarios. Based on the experimental data on the concentration dependence, the sizes of the folding nuclei of fibrils were calculated. It turned out that the size of the primary nucleus is one "monomer" and the size of the secondary nucleus is zero. This means that the nucleus for new aggregates can be a surface of the fibrils themselves. Using electron microscopy, we have demonstrated that fibrils of these peptides are formed by the association of rounded ring structures. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|