Neurodegeneration Pathways: Amyloid, Tau & Proteinopathy Mechanisms
The study of protein misfolding and aggregation remains central to understanding neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Abnormal accumulation of proteins including amyloid-β, tau, α-synuclein, and TDP-43 disrupts synaptic signaling, triggers inflammation, and leads to neuronal death. Research continues to unravel the mechanisms driving aggregation, impaired proteostasis, mitochondrial dysfunction, oxidative stress, and lysosomal system failure. Innovations in molecular pathway mapping allow targeted disruption of toxic aggregates, stabilization of native protein structures, and enhancement of proteolytic clearance mechanisms. Novel therapeutics, including immunotherapies, molecular inhibitors, antisense RNA agents, and gene-based interventions, aim to prevent aggregation, neutralize toxic species, and preserve neuronal integrity. Understanding proteinopathy dynamics is essential for developing disease-modifying treatments and slowing progression across multiple neurodegenerative conditions.
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