Abstract
Phthalocyanine tetrasulfonates are known to interact with mammalian prion protein, having the ability to act as anti-prion agents and help prevent the conversion of native isoform PrPc to the scrapie isoform PrPsc. However, the interaction between phthalocyanines and PrP remains poorly characterized. We explore the phenomenology of this interaction in detail by examining the binding of phthalocyanines to monomeric native Syrian Hamster prion protein using multiple complementary assays: surface plasmon resonance, FCS, fluorescence quenching, calorimetry, and CD spectroscopy. We determine binding constants, kinetics, stoichiometry, structural and spectroscopic effects of binding, and the influence of buffer ionic strength.
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