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.

Original languageEnglish
Pages (from-to)450-463
Number of pages14
JournalBiochemistry (Moscow)
Issue number5
StatePublished - May 2022

    Scopus subject areas

  • Geriatrics and Gerontology
  • Biochemistry, Genetics and Molecular Biology (miscellaneous)
  • Biophysics
  • Biochemistry

    Research areas

  • amyloid polymorphism, amyloid-like aggregates, amyloids, cross-β structure, Amyloid/metabolism, Amyloidosis/genetics, Humans, Protein Conformation, Amyloidogenic Proteins, Polymorphism, Genetic

ID: 97488764