| Literature DB >> 32277934 |
Jordi Pujols1, Samuel Peña-Díaz2, Irantzu Pallarès2, Salvador Ventura3.
Abstract
Parkinson's disease (PD) is characterized by progressive loss of dopaminergic neurons and the accumulation of deposits of α-synuclein (α-syn) in the brain. The pivotal role of α-syn aggregation in PD makes it an attractive target for potential disease-modifying therapies. However, the disordered nature of the protein, its multistep aggregation mechanism, and the lack of structural information on intermediate species complicate the discovery of modulators of α-syn amyloid deposition. Despite these difficulties, small molecules have been shown to block the misfolding and aggregation of α-syn, and can even disentangle mature α-syn amyloid fibrils. In this review we provide an updated overview of these leading small compounds and discuss how these chemical chaperones hold great promise to alter the course of PD progression.Entities:
Keywords: Parkinson’s disease; amyloid fibril; disease-modifying therapy; protein aggregation; small molecule; α-synuclein
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Year: 2020 PMID： 32277934 DOI： 10.1016/j.molmed.2020.01.005
Source DB: PubMed Journal: Trends Mol Med ISSN： 1471-4914 Impact factor: 11.951