Photocatalytic degradation of prions using the photo-Fenton reagent.
Prions are proteinaceous infectious agents postulated to be the causative agents of a group of fatal neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). A known iatrogenic transmission route of TSEs to humans occurs via prion-contaminated surgical instruments or biological materials. Prions, unlike most common pathogens, exhibit an extraordinary resistance to conventional decontamination procedures. We have recently demonstrated that the application of TiO(2)-based heterogeneous photocatalytic oxidation is able to significantly reduce prion infectivity. The present study investigates the potential of a homogeneous photocatalytic method, based on the photo-Fenton reagent, to degrade prion proteins. We show that the photo-Fenton reagent efficiently degrades not only recombinant prion proteins, but also the total protein amount from brain preparations of naturally or experimentally infected species and PrP(Sc) (PrP scrapie) contained in sheep scrapie brain homogenates.
Paspaltsis
I
I
Laboratory of Pharmacology, School of Pharmacy, Aristotle University of Thessaloniki, Thessaloniki, Greece.
Berberidou
C
C
Poulios
I
I
Sklaviadis
T
T
D000818:Animals; D003666:Decontamination / Q000379:methods*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D007501:Iron / Q000494:pharmacology*; D055668:Photochemical Processes; D018620:PrPSc Proteins / Q000187:drug effects*; D012608:Scrapie / Q000517:prevention & control*; D034561:Sheep, Domestic; D014466:Ultraviolet Rays
C045076:Fenton's reagent; D018620:PrPSc Proteins; D006861:Hydrogen Peroxide; D007501:Iron