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Glycosaminoglycans (GAGs) bind to amyloidogenic precursor proteins, such as amyloid-β precursor protein (APP), primarily through electrostatic interactions, promoting conformational changes and aggregation into β-sheet-rich oligomers and mature amyloid fibrils. GAGs act as structural templates that facilitate nucleation, aggregation, and stabilization of these fibrils, potentially impeding clearance. This interaction plays a central role in the pathogenesis and progression of systemic and localized forms of amyloidosis, including Alzheimer's disease, making it a potential therapeutic target. Disrupting or inhibiting this interaction has shown promise in reducing pathological aggregation.
Inhibition of GAG biosynthesis or binding to amyloidogenic proteins.
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