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Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates

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Abstract

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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Abbreviations

Aβ:

β-amyloid

Cryo-EM:

cryogenic electron microscopy

LARKS:

low-complexity aromatic-rich kinked segment

PHF:

paired helical filament

PrP:

prion protein

SF:

straight filament

TTR:

transthyretin

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Funding

This work was supported by the Russian Foundation for Basic Research (project no. 20-34-90117).

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Authors and Affiliations

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

    Anton B. Matiiv, Nina P. Trubitsina, Andrew G. Matveenko, Yury A. Barbitoff, Galina A. Zhouravleva & Stanislav A. Bondarev

  2. Bioinformatics Institute, 197342, Saint Petersburg, Russia

    Yury A. Barbitoff

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

    Galina A. Zhouravleva & Stanislav A. Bondarev

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Matiiv, A.B., Trubitsina, N.P., Matveenko, A.G. et al. Structure and Polymorphism of Amyloid and Amyloid-Like Aggregates. Biochemistry Moscow 87, 450–463 (2022). https://doi.org/10.1134/S0006297922050066

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