The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation
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...
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| Format: | Article |
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MDPI AG
2023-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/4/3781 |
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| author | Oxana V. Galzitskaya Sergei Y. Grishin Anna V. Glyakina Nikita V. Dovidchenko Anastasiia V. Konstantinova Sergey V. Kravchenko Alexey K. Surin |
| author_facet | Oxana V. Galzitskaya Sergei Y. Grishin Anna V. Glyakina Nikita V. Dovidchenko Anastasiia V. Konstantinova Sergey V. Kravchenko Alexey K. Surin |
| author_sort | Oxana V. Galzitskaya |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-11T08:41:59Z |
| format | Article |
| id | doaj.art-80598d57af4949f9ac2e281e2dd2d39d |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T08:41:59Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-80598d57af4949f9ac2e281e2dd2d39d2023-11-16T21:04:56ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-02-01244378110.3390/ijms24043781The Strategies of Development of New Non-Toxic Inhibitors of Amyloid FormationOxana V. Galzitskaya0Sergei Y. Grishin1Anna V. Glyakina2Nikita V. Dovidchenko3Anastasiia V. Konstantinova4Sergey V. Kravchenko5Alexey K. Surin6Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaInstitute of Environmental and Agricultural Biology (X-BIO), Tyumen State University, 625003 Tyumen, RussiaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, RussiaIn 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.https://www.mdpi.com/1422-0067/24/4/3781amyloidα-synucleininsulinamyloid-betaAlzheimer’s diseaseParkinson’s disease |
| spellingShingle | Oxana V. Galzitskaya Sergei Y. Grishin Anna V. Glyakina Nikita V. Dovidchenko Anastasiia V. Konstantinova Sergey V. Kravchenko Alexey K. Surin The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation International Journal of Molecular Sciences amyloid α-synuclein insulin amyloid-beta Alzheimer’s disease Parkinson’s disease |
| title | The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation |
| title_full | The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation |
| title_fullStr | The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation |
| title_full_unstemmed | The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation |
| title_short | The Strategies of Development of New Non-Toxic Inhibitors of Amyloid Formation |
| title_sort | strategies of development of new non toxic inhibitors of amyloid formation |
| topic | amyloid α-synuclein insulin amyloid-beta Alzheimer’s disease Parkinson’s disease |
| url | https://www.mdpi.com/1422-0067/24/4/3781 |
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