| Autor: |
Matiiv AB; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia., Trubitsina NP; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia., Matveenko AG; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia., Barbitoff YA; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia.; Bioinformatics Institute, Saint Petersburg, 197342, Russia., Zhouravleva GA; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia.; Laboratory of Amyloid Biology, Saint Petersburg State University, Saint Petersburg, 199034, Russia., Bondarev SA; Department of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, 199034, Russia. stanislavspbgu@gmail.com.; Laboratory of Amyloid Biology, Saint Petersburg State University, Saint Petersburg, 199034, Russia. |
| Abstrakt: |
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. |
