Prion disease is a rapidly progressive neurodegenerative disorder caused by misfolding
and aggregation of the prion protein (PrP), and there are currently no therapeutic options.
PrP ligands could theoretically antagonize prion formation by protecting the native protein
from misfolding or by targeting it for degradation, but no validated small-molecule binders
have been discovered to date. We deployed a variety of screening methods in an effort to
discover binders of PrP, including 19 F-observed and saturation transfer difference (STD) …