REVIEW: Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates

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Anton B. Matiiv¹, Nina P. Trubitsina¹, Andrew G. Matveenko¹, Yury A. Barbitoff^1,2, Galina A. Zhouravleva^1,3, and Stanislav A. Bondarev^1,3,a*

¹Department of Genetics and Biotechnology, Saint Petersburg State University, 199034 Saint Petersburg, Russia

²Bioinformatics Institute, 197342 Saint Petersburg, Russia

³Laboratory of Amyloid Biology, Saint Petersburg State University, 199034 Saint Petersburg, Russia

^* To whom correspondence should be addressed.

Received September 28, 2021; Revised April 8, 2022; Accepted April 9, 2022

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Amyloids are protein aggregates with the cross-β structure. The interest in amyloids is explained, on the one hand, by their role in the development of socially significant human neurodegenerative diseases, and on the other hand, by the discovery of functional amyloids, whose formation is an integral part of cellular processes. To date, more than a hundred proteins with the amyloid or amyloid-like properties have been identified. Studying the structure of amyloid aggregates has revealed a wide variety of protein conformations. In the review, we discuss the diversity of protein folds in the amyloid-like aggregates and the characteristic features of amyloid aggregates that determine their unusual properties, including stability and interaction with amyloid-specific dyes. The review also describes the diversity of amyloid aggregates and its significance for living organisms.

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KEY WORDS: cross-β structure, amyloids, amyloid-like aggregates, amyloid polymorphism

DOI: 10.1134/S0006297922050066

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