AI Article Synopsis
- - Alzheimer's disease is marked by amyloid-beta peptide (Aβ) forming harmful plaques in the brain, which may worsen the disease.
- - The amyloid hypothesis suggests that treatments preventing Aβ aggregation or reducing plaques could alter the disease's course; in 2023, the FDA approved lecanemab, a monoclonal antibody targeting Aβ aggregates.
- - This review explores the role of interactions between zinc ions, a specific Aβ variant (isoD7-Aβ), and a receptor in Aβ aggregation, using various transgenic animal models for research insights.
Article Abstract
A hallmark of Alzheimer's disease (AD) are the proteinaceous aggregates formed by the amyloid-beta peptide (Aβ) that is deposited inside the brain as amyloid plaques. The accumulation of aggregated Aβ may initiate or enhance pathologic processes in AD. According to the amyloid hypothesis, any agent that has the capability to inhibit Aβ aggregation and/or destroy amyloid plaques represents a potential disease-modifying drug. In 2023, a humanized IgG1 monoclonal antibody (lecanemab) against the Aβ-soluble protofibrils was approved by the US FDA for AD therapy, thus providing compelling support to the amyloid hypothesis. To acquire a deeper insight on the in vivo Aβ aggregation, various animal models, including aged herbivores and carnivores, non-human primates, transgenic rodents, fish and worms were widely exploited. This review is based on the recent data obtained using transgenic animal AD models and presents experimental verification of the critical role in Aβ aggregation seeding of the interactions between zinc ions, Aβ with the isomerized Asp7 (isoD7-Aβ) and the α4β2 nicotinic acetylcholine receptor.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10778642 | PMC |
| http://dx.doi.org/10.3390/ijms25010072 | DOI Listing |
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