The small molecule ZPD‐2 inhibits the aggregation and seeded polymerisation of C‐terminally truncated α‐Synuclein

Protein aggregation, particularly the formation of amyloid fibrils, is associated with numerous human disorders, including Parkinson's disease. This neurodegenerative condition is characterised by the accumulation of α‐Synuclein amyloid fibrils within intraneuronal deposits known as Lewy bodies...

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Veröffentlicht in:	The FEBS journal 2024-12, Vol.291 (23), p.5290-5304
Hauptverfasser:	Peña‐Díaz, Samuel, Ventura, Salvador
Format:	Artikel
Sprache:	eng
Schlagworte:	alpha-Synuclein - chemistry alpha-Synuclein - genetics alpha-Synuclein - metabolism amyloid Amyloid - chemistry Amyloid - genetics Amyloid - metabolism Axons Benzodioxoles Bioaccumulation Fibrillogenesis Humans Inclusions inhibition Intermediates Lewy bodies Movement disorders neurites Neurodegenerative diseases Neurological Diseases oligomer Original Parkinson disease Parkinson Disease - drug therapy Parkinson Disease - genetics Parkinson Disease - metabolism Parkinson Disease - pathology Parkinson's Disease Pathogenesis Polymerization Protein Protein Aggregates - drug effects protein aggregation Protein Aggregation, Pathological - genetics Protein Aggregation, Pathological - metabolism Protein Aggregation, Pathological - pathology Protein interaction Protein Multimerization - drug effects Pyrazoles Synuclein therapeutics truncation α‐Synuclein
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