| Autor: |
Galzitskaya OV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia., Grishin SY; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; Institute of Environmental and Agricultural Biology (X-BIO), Tyumen State University, 625003 Tyumen, Russia., Glyakina AV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; Institute of Mathematical Problems of Biology RAS, The Branch of Keldysh Institute of Applied Mathematics, Russian Academy of Sciences, 142290 Pushchino, Russia., Dovidchenko NV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia., Konstantinova AV; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; Faculty of Biotechnology, Lomonosov Moscow State University, 119991 Moscow, Russia., Kravchenko SV; Institute of Environmental and Agricultural Biology (X-BIO), Tyumen State University, 625003 Tyumen, Russia., Surin AK; Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.; The Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.; State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Russia. |
| Abstrakt: |
In recent years, due to the aging of the population and the development of diagnostic medicine, the number of identified diseases associated with the accumulation of amyloid proteins has increased. Some of these proteins are known to cause a number of degenerative diseases in humans, such as amyloid-beta (Aβ) in Alzheimer's disease (AD), α-synuclein in Parkinson's disease (PD), and insulin and its analogues in insulin-derived amyloidosis. In this regard, it is important to develop strategies for the search and development of effective inhibitors of amyloid formation. Many studies have been carried out aimed at elucidating the mechanisms of amyloid aggregation of proteins and peptides. This review focuses on three amyloidogenic peptides and proteins-Aβ, α-synuclein, and insulin-for which we will consider amyloid fibril formation mechanisms and analyze existing and prospective strategies for the development of effective and non-toxic inhibitors of amyloid formation. The development of non-toxic inhibitors of amyloid will allow them to be used more effectively for the treatment of diseases associated with amyloid. |
