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Influence of Chaperones on Amyloid Formation of Аβ Peptideстатья
- Авторы: Galzitskaya O.V., Selivanova O.M., Dzhus U.F., Marchenkov V.V., Suvorina M.Yu, Surin A.K.
- Журнал: Current Protein and Peptide Science
- Том: 23
- Номер: 1
- Год издания: 2022
- Издательство: Bentham Science Publishers
- Местоположение издательства: Netherlands
- Первая страница: 44
- Последняя страница: 51
- DOI: 10.2174/1389203723666220127152545
- Аннотация: An extensive study of the folding and stability of proteins and their complexes has revealed a number of problems and questions to be answered. One of them is the effect of chaperones on the process of fibrillation of various proteins and peptides. We studied the effect of molecular chaperones, such as α-crystallin and GroEL, on the fibrillogenesis of Aβ(1-42) peptide. Recombinant GroEL and Aβ(1-42) was isolated and purified. It was shown that the assembly of GroEL occurs without the addition of magnesium and ATP ions, as was commonly believed. According to the electron microscopy results, GroEL insignificantly affects the fibrillogenesis of the Aβ(1-42) peptide, while α-crystallin prevents the elongation of the Aβ(1-42) peptide fibrils. The data obtained will help us understand the process of amyloid formation and the influence of various components on it.
- Добавил в систему: Галзитская Оксана Валериановна