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Tau protein is a microtubule-associated protein predominantly found in neurons, where it stabilizes microtubules and supports cell architecture and transport. In neurodegenerative diseases, tau can become hyperphosphorylated, detach from microtubules, and form insoluble neurofibrillary tangles, leading to neuronal dysfunction and death. Amyloid-β peptide is a proteolytic fragment generated from amyloid precursor protein (APP) through β- and γ-secretase cleavage. It aggregates into extracellular plaques, forming β-sheet-rich amyloid fibrils in the brain tissue of Alzheimer's disease patients. Both toxins can self-propagate and spread through prion-like mechanisms. While amyloid-β aggregation has long been the dominant therapeutic target, recent evidence highlights the role of tau pathology and its interplay with amyloid-β in disease progression. Clinical trials continue to evaluate therapies targeting these proteins, but long-term efficacy and safety remain subjects of ongoing research.
Amyloid-targeting antibodies bind and promote clearance of aggregated Aβ plaques. Secretase inhibitors block the production of Aβ by inhibiting β- or γ-secretases. Tau-targeting therapies inhibit tau hyperphosphorylation, aggregation, or promote clearance of tau tangles.
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