SPR biosensor as a tool for screening prion protein binders as potential antiprion leads.
Prion diseases, also called transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative disorders affecting animals and humans. No effective treatments are currently available for the diseases, vCJD in particular. It is believed that the formation of protease-resistant insoluble prion protein (PrP(Sc)), which is the main component of amyloidal deposits, from the cellular prion protein (PrP(C)), is essential for the progression of the disease. Therefore, both PrP(Sc) and PrP(C) are currently being used as potential drug targets.This protocol details an optimised experimental protocol to conduct an affinity screening of compound libraries by the immobilisation of PrP(C) using an SPR-based instrument, Biacore 3000.
Chen
Beining
B
Department of Chemistry, University of Sheffield, Sheffield, UK.
D004353:Drug Evaluation, Preclinical / Q000295:instrumentation / Q000379:methods*; D006801:Humans; D055767:Immobilized Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D011328:Prions / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D054852:Small Molecule Libraries / Q000378:metabolism / Q000494:pharmacology; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods*
D055767:Immobilized Proteins; D011328:Prions; D011994:Recombinant Proteins; D054852:Small Molecule Libraries