Influence of Chaperones on Amyloid Formation of Аβ Peptide.

Autor:	Galzitskaya OV; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia.; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino Moscow Region, Russia., Selivanova OM; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia., Dzhus UF; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia., Marchenkov VV; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia., Suvorina MY; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia., Surin AK; Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya str., Pushchino, Moscow Region, 142290, Russia.; State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk Moscow Region, Russia.; The Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino Moscow Region, Russia.
Jazyk:	angličtina
Zdroj:	Current protein & peptide science [Curr Protein Pept Sci] 2022; Vol. 23 (1), pp. 44-51.
DOI:	10.2174/1389203723666220127152545
Abstrakt:	Background: 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. Methods: 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. Results: 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. Conclusion: The data obtained will help us understand the process of amyloid formation and the effect of various components on it. (Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.)
Databáze:	MEDLINE
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