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Updated: Jul 28, 2025
Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
Published on: May 13, 2010
Protein Interactome of Amyloid-β as a Therapeutic Target
Vladimir F Lazarev1, Elizaveta A Dutysheva1, Igor E Kanunikov2
1Institute of Cytology of the Russian Academy of Sciences, 194064 Saint Petersburg, Russia.
Abstract:
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.
Insights
Alzheimer's disease (AD) involves beta-amyloid (Aβ) peptide toxicity, often worsened by interactions with proteins like tau and APOE. This review explores compounds targeting Aβ complexes to reduce AD pathogenesis.
Area of Science:
- Neuroscience
- Biochemistry
- Pathology
Background:
- The amyloid concept posits beta-amyloid (Aβ) peptide as central to Alzheimer's disease (AD) pathogenesis.
- Aβ peptide injures neural cells, leading to malfunction and death.
- Aβ toxicity is modulated by interacting proteins such as tau, APOE, and transthyretin.
Purpose of the Study:
- To review data on Aβ-based complexes in AD pathogenesis.
- To discuss compounds targeting Aβ or its complexes with other polypeptides.
Main Methods:
- Literature review of studies on Aβ interactions and therapeutic targets.
- Analysis of Aβ co-factor roles in modulating peptide aggregation and toxicity.
Main Results:
- Aβ toxicity is significantly influenced by its interactions with other brain proteins.
- These interactions affect Aβ oligomerization and aggregation, thereby modulating neurotoxicity.
- Specific compounds targeting Aβ or its complexes show potential for reducing AD pathology.
Conclusions:
- Targeting Aβ-peptide interactions with co-factors is a promising therapeutic strategy for AD.
- Developing compounds that prevent pathogenic Aβ interactions could mitigate AD progression.
- Further research into Aβ-protein complexes may reveal novel therapeutic avenues for Alzheimer's disease.
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