A Promising Antiprion Trimethoxychalcone Binds to the Globular Domain of the Cellular Prion Protein and Changes Its Cellular Location.

ABSTRACT: The search for antiprion compounds has been encouraged by the fact that transmissible spongiform encephalopathies (TSEs) share molecular mechanisms with more prevalent neurodegenerative pathologies, such as Parkinson's and Alzheimer's diseases. Cellular prion protein (PrP^C) conversion into protease-resistant forms (protease-resistant PrP [PrP^Res] or the scrapie form of PrP [PrP^Sc]) is a critical step in the development of TSEs and is thus one of the main targets in the screening for antiprion compounds. In this work, three trimethoxychalcones (compounds J1, J8, and J20) and one oxadiazole (compound Y17), previously identified in vitro to be potential antiprion compounds, were evaluated through different approaches in order to gain inferences about th

SUBMITTER: Ferreira NC 

PROVIDER: S-EPMC5786768 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature