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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.