The small molecule ZPD-2 inhibits the aggregation and seeded polymerisation of C-terminally truncated a-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 alpha-Synuclein amyloid fibrils within intraneuronal deposits known as Lewy bo...
| Autores: | , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Institut d'Investigació i Innovació Parc Taulí (I3PT) |
| Repositorio: | r-I3PT. Repositorio Institucional Producción Científica del Institut d'Investigació i Innovació Parc Taulí |
| OAI Identifier: | oai:i3pt.fundanetsuite.com:p5310 |
| Acceso en línea: | https://i3pt.portalinvestigacion.com/publicaciones/5310 https://www.scopus.com/inward/record.uri?eid=2-s2.0-85207786636&doi=10.1111%2ffebs.17310&partnerID=40&md5=f972a9bd9168280c7e6f17f55711cd80 |
| Access Level: | acceso abierto |
| Palabra clave: | inhibition oligomer protein aggregation truncation alpha-Synuclein |
| Sumario: | 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 alpha-Synuclein amyloid fibrils within intraneuronal deposits known as Lewy bodies or neurites. C-terminally truncated forms of alpha-Synuclein are frequently observed in these inclusions in the brains of patients, and their increased aggregation propensity suggests a role in the disease's pathogenesis. This study demonstrates that the small molecule ZPD-2 acts as a potent inhibitor of both the spontaneous and seeded amyloid polimerisation of C-terminally truncated alpha-Synuclein by interfering with early aggregation intermediates. This dual activity positions this molecule as a promising candidate for therapeutic development in treating synucleinopathies. |
|---|