Influence of Chaperones on Amyloid Formation of Аβ Peptide

• Published in: Current protein & peptide science Vol. 23; no. 1; p. 44
• Main Authors: Galzitskaya, O V, Selivanova, O M, Dzhus, U F, Marchenkov, V V, Suvorina, M Yu, Surin, A K
• Format: Journal Article
• Language: English
• Published: United Arab Emirates 2022
• Subjects: alpha-Crystallins; Amyloid - chemistry; Amyloid beta-Peptides - metabolism; Amyloidogenic Proteins; Amyloidosis; Humans; Molecular Chaperones - genetics; Peptide Fragments - chemistry; Aggregation; electron microscopy; mass spectrometry; nucleus; chaperones; fibrils
• ISSN: 1875-5550
• DOI: 10.2174/1389203723666220127152545

An extensive study of the folding and stability of proteins and their complexes has revealed a number of problems and questions that need 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 GroEL and α-crystallin, on the fibrillogenesis of the Aβ(1-42) peptide using electron microscopy and surface plasmon resonance.
Recombinant GroEL and Aβ(1-42) were isolated and purified. It was shown that the assembly of GroEL occurs without the addition of magnesium and potassium ions, as is 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. We have demonstrated that GroEL interacts nonspecifically with Aβ(1-42), while α-crystallin does not interact with Aβ(1-42) at all using surface plasmon resonance.
The data obtained will help us understand the process of amyloid formation and the effect of various components on it.