REVIEW: Factors Affecting Pathological Amyloid Protein Transformation: From Post-Translational Modifications to Chaperones

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Vladimir I. Muronets^1,2,3,a*, Sofiya S. Kudryavtseva¹, Lidia P. Kurochkina¹, Evgeniia V. Leisi³, Yulia Yu. Stroylova^1,3, Elena V. Schmalhausen¹

¹Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia

²Butlerov Institute of Chemistry, Kazan (Volga Region) Federal University, 420008 Kazan, Russia

³Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119991 Moscow, Russia

^* To whom correspondence should be addressed.

Received: September 20, 2024; Revised: October 10, 2024; Accepted: October 30, 2024

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The review discusses the influence of various factors (e.g., post-translational modifications and chaperones) on the pathological transformation of amyloidogenic proteins involved in the onset and development of neurodegenerative diseases (Alzheimer’s and Parkinson’s diseases) and spongiform encephalopathies of various origin with special focus on the role of α-synuclein, prion protein, and, to a lesser extent, beta-amyloid peptide. The factors investigated by the authors of this review are discussed in more detail, including posttranslational modifications (glycation and S-nitrosylation), cinnamic acid derivatives and dendrimers, and chaperonins (eukaryotic, bacterial, and phage). A special section is devoted to the role of the gastrointestinal microbiota in the pathogenesis of amyloid neurodegenerative diseases, in particular, its involvement in the transformation of infectious prions and possibly other proteins capable of prion-like transmission of amyloidogenic diseases.

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KEY WORDS: β-amyloid, prion protein, α-synuclein, microbiota, chaperons, post-translational modifications

DOI: 10.1134/S0006297924604003

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