Prions are the etiological agents of transmissible spongiform encephalopathies, a class of fatal neurodegenerative diseases that affect humans, deer, sheep, and cattle. Prion diseases of deer and sheep can be transmitted indirectly via environmental routes. Strong evidence suggests that soil may serve as a reservoir of prion infectivity, which can persist in the environment for years. Here, we investigated the attachment of pathogenic prion protein to humic acid surfaces using a combination of label-free, in situ techniques: quartz crystal microbalance with dissipation monitoring and optical waveguide light mode spectroscopy. Humic acid-coated surfaces were prepared by electrostatic layer-by-layer assembly. The extent and reversibility of pathogenic prion protein attachment was examined as a function of solution pH, ionic strength, and physicochemical properties of the humic acid. Our findings are consistent with a dominant role of electrostatics in the interaction of pathogenic prion protein and humic acid fillms. Humic acid polarity also appeared to influence pathogenic prion protein attachment.

Attachment of pathogenic prion protein to humic substances

248th National Meeting (2014)

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