Synthesis and anti-prion aggregation activity of acylthiosemicarbazide analogues.

ABSTRACT: Prions are infectious protein particles known to cause prion diseases. The biochemical entity of the pathogen is the misfolded prion protein (PrP^Sc) that forms insoluble amyloids to impair brain function. PrP^Sc interacts with the non-pathogenic, cellular prion protein (PrP^C) and facilitates conversion into a nascent misfolded isoform. Several small molecules have been reported to inhibit the aggregation of PrP^Sc but no pharmacological intervention was well established thus far. We, here, report that acylthiosemicarbazides inhibit the prion aggregation. Compounds 7x and 7y showed almost perfect inhibition (EC₅₀ = 5 µM) in prion aggregation formation assay. The activity was further confirmed by atomic force microscopy, semi

SUBMITTER: Kim DH 

PROVIDER: S-EPMC10038035 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature