Targeting Protein Misfolding and Aggregation as a Therapeutic Perspective in Neurodegenerative Disorders
Marta Sidoryk-Węgrzynowicz1, Kamil Adamiak1, Lidia Strużyńska1
1Laboratory of Pathoneurochemistry, Department of Neurochemistry, Mossakowski Medical Research Institute, 02-106 Warsaw, Poland.
International Journal of Molecular Sciences
|November 27, 2024
Summary
Abnormal protein misfolding and spreading drive neurodegenerative diseases like Parkinson's and Alzheimer's. Inhibiting these processes offers a promising therapeutic strategy for these conditions.
Area of Science:
- Neuroscience
- Pathology
- Pharmacology
Background:
- Abnormal protein deposition and spread are central to neurodegenerative disease pathogenesis.
- Protein oligomers and filaments are key in diseases like synucleinopathies (e.g., Parkinson's disease) and tauopathies (e.g., Alzheimer's disease).
Purpose of the Study:
- To review mechanisms of protein-dependent neurodegeneration.
- To describe current therapeutic strategies targeting protein misfolding and aggregation.
Main Methods:
- Literature review of common neurodegenerative disorders.
- Analysis of therapeutic approaches targeting pathological protein forms.
Main Results:
- Synucleinopathies and tauopathies involve specific protein aggregation pathways.
- Inhibition of protein misfolding and interneuronal spread is a promising therapeutic avenue.
Conclusions:
- Targeting pathological protein mechanisms is crucial for treating neurodegenerative disorders.
- Developing therapies to inhibit protein misfolding and aggregation holds significant potential for disease modification.
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