Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a family of neurodegenerative disorders caused by the misfolded version of the mammalian prion protein (PrP). Due to the extreme stability of these misfolded proteins, their release into the environment through shedding or carcass decomposition has been implicated in the spread of TSEs in some wild and domestic animal species. Current understanding of PrP attachment to environmental surfaces is limited. Using the quartz crystal microbalance with dissipation monitoring, we studied PrP interactions with humic acid- and mineral-coated surfaces that prions are likely to encounter ex vivo as a function of solution composition. PrP interaction with humic acid exhibits pronounced pH dependency. The influence of humic acid composition and protein structure on PrP attachment to humic acid-coated and mineral surfaces will be discussed.

Probing pathogenic prion protein interactions with humic acid and mineral surfaces using the quartz crystal microbalance with dissipation

239th National Meeting (2010)

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