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Amyloid protein aggregation is the process by which normally soluble proteins misfold and assemble into insoluble, highly ordered fibrillar aggregates known as amyloids. These aggregates are characterized by a cross-β-sheet structure and are implicated in a range of diseases, including Alzheimer’s disease, Parkinson’s disease, type 2 diabetes, and various systemic amyloidoses. The process involves primary nucleation, elongation, secondary nucleation and fragmentation. Therapeutic strategies focus on inhibiting these steps, stabilizing native protein conformations or enhancing clearance of misfolded species.
Inhibition of primary nucleation or elongation steps; Stabilization of native protein conformations; Enhancement of clearance/degradation pathways
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