High-throughput screening methodology to identify alpha-synuclein aggregation inhibitors

An increasing number of neurodegenerative diseases are being found to be associated with the abnormal accumulation of aggregated proteins in the brain. In Parkinson's disease, this process involves the aggregation of alpha-synuclein (α-syn) into intraneuronal inclusions. Thus, compounds that in...

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Detalles Bibliográficos
Autores: Pujols Pujol, Jordi|||0000-0001-9424-5866, Peña Díaz, Samuel|||0000-0002-2902-823X, Conde Giménez, María|||0000-0003-4358-9110, Garcia de Carvalho Pinheiro, Francisca|||0000-0003-3778-1528, Navarro, Susanna|||0000-0001-8160-9536, Sancho Sanz, Javier|||0000-0002-2879-9200, Ventura, Salvador|||0000-0002-9652-6351
Tipo de recurso: artículo
Fecha de publicación:2017
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:186171
Acceso en línea:https://ddd.uab.cat/record/186171
https://dx.doi.org/urn:doi:10.3390/ijms18030478
Access Level:acceso abierto
Palabra clave:High-throughput screening
α-synuclein
Parkinson disease
Amyloid
Protein aggregation
Descripción
Sumario:An increasing number of neurodegenerative diseases are being found to be associated with the abnormal accumulation of aggregated proteins in the brain. In Parkinson's disease, this process involves the aggregation of alpha-synuclein (α-syn) into intraneuronal inclusions. Thus, compounds that inhibit α-syn aggregation represent a promising therapeutic strategy as disease-modifying agents for neurodegeneration. The formation of α-syn amyloid aggregates can be reproduced in vitro by incubation of the recombinant protein. However, the in vitro aggregation of α-syn is exceedingly slow and highly irreproducible, therefore precluding fast high throughput anti-aggregation drug screening. Here, we present a simple and easy-to-implement in-plate method for screening large chemical libraries in the search for α-syn aggregation modulators. It allows us to monitor aggregation kinetics with high reproducibility, while being faster and requiring lower protein amounts than conventional aggregation assays. We illustrate how the approach enables the identification of strong aggregation inhibitors in a library of more than 14,000 compounds.