| Autor: |
Lazarev VF; Institute of Cytology of the Russian Academy of Sciences, 194064 Saint Petersburg, Russia., Dutysheva EA; Institute of Cytology of the Russian Academy of Sciences, 194064 Saint Petersburg, Russia., Kanunikov IE; Biological Faculty, St. Petersburg State University, 199034 Saint Petersburg, Russia., Guzhova IV; Institute of Cytology of the Russian Academy of Sciences, 194064 Saint Petersburg, Russia., Margulis BA; Institute of Cytology of the Russian Academy of Sciences, 194064 Saint Petersburg, Russia. |
| Jazyk: |
angličtina |
| Zdroj: |
Pharmaceuticals (Basel, Switzerland) [Pharmaceuticals (Basel)] 2023 Feb 16; Vol. 16 (2). Date of Electronic Publication: 2023 Feb 16. |
| DOI: |
10.3390/ph16020312 |
| Abstrakt: |
The amyloid concept of Alzheimer's disease (AD) assumes the β-amyloid peptide (Aβ) as the main pathogenic factor, which injures neural and other brain cells, causing their malfunction and death. Although Aβ has been documented to exert its cytotoxic effect in a solitary manner, there is much evidence to claim that its toxicity can be modulated by other proteins. The list of such Aβ co-factors or interactors includes tau, APOE, transthyretin, and others. These molecules interact with the peptide and affect the ability of Aβ to form oligomers or aggregates, modulating its toxicity. Thus, the list of potential substances able to reduce the harmful effects of the peptide should include ones that can prevent the pathogenic interactions by specifically binding Aβ and/or its partners. In the present review, we discuss the data on Aβ-based complexes in AD pathogenesis and on the compounds directly targeting Aβ or the destructors of its complexes with other polypeptides. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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