Samuel Peña-Díaz

TL;DR: High-throughput screening methodology is exploited to identify SynuClean-D, a small compound that inhibits α-synuclein aggregation, disrupts mature amyloid fibrils, prevents fibril propagation, and abolishes the degeneration of dopaminergic neurons in an animal model of Parkinson’s disease.

TL;DR: The Database of Intrinsically Disordered Proteins (DisProt) as discussed by the authors is a repository of manually curated annotations of intrinsically disordered proteins and regions from the literature, including a restyled web interface.

TL;DR: A simple and easy-to-implement in-plate method for screening large chemical libraries in the search for α-syn aggregation modulators that allows us to monitor aggregation kinetics with high reproducibility, while being faster and requiring lower protein amounts than conventional aggregation assays.

TL;DR: An updated overview of the leading small compounds shown to block the misfolding and aggregation of α-syn, and how these chemical chaperones hold great promise to alter the course of PD progression is provided.

TL;DR: In this paper, the authors exploit the biophysical properties of toxic oligomers and amyloid fibrils to identify a family of αhelical peptides that bind to these α-synuclein species with low nanomolar affinity, without interfering with the monomeric functional protein.