We defined the mechanism of inhibition of PrP conversion by curcumin, the active ingredient of spice turmeric. We showed binding of curcumin to both toxic ß-oligomers as well as to amyloid fibrils. Curcumin bound to partially unfolded ?-form PrP, formed at acidic pH, but not to the native PrP. This is the first description of a nontoxic compound of natural source binding to the partially unfolded intermediate of the prion protein. Our results are important for potential use of curcumin and its derivates with improved pharmacological features for diagnosis and therapy of amyloid diseases.
COBISS.SI-ID: 3896346
The structural conversion of prion protein occurring in prion disease is not well characterized, especially due to the lack of knowledge on the structure of pathological form, PrPSc. Thus a comprehensive set of well characterized antibodies directed against various epitopes on PrP might prove invaluable in obtaining structural information on PrPSc and characterization of prion strains. We also show that this antibody set can be used in various experimental platforms, which even broadens its applicability in basic research and diagnostics.
COBISS.SI-ID: 4096794