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  • Tetracysteine-tagged prion protein allows discrimination between the native and converted forms
    Gašperšič, Jernej ...
    The conformational conversion of prion protein (PrP) from a native conformation to the amyloid form is a hallmark of transmissible spongiform encephalopathies. Conversion is usually monitored by ... fluorescent dyes, which bind generic amyloids and are less suited for living cell imaging. We report a new method for the synthesis of membrane-permeable and membrane-impermeable biarsenical reagents, which are then used to monitor murine PrP (mPrP) misfolding. We introduced tetracysteine (TC) tags into three different positions of mPrP, which folded into a native-like structure. Whereas mPrPs with a TC tag inserted at the N-terminus or C-terminus supported fibril formation, insertion into the helix 2-helix 3 loop inhibited conversion. We devised a quantitative protease-free method to determine the fraction of converted PrP, based on the ability of the fluorescein arsenical helix binder reagent to differentiate between the monomeric and fibrilized form of TC-tagged PrP, and showed that TC-tagged mPrP could be detected on transfectedcells, thereby expanding the potential use of this method for the detection and study of conformational diseases.
    Vir: FEBS journal. - ISSN 1742-464X (Vol. 277, no. 9, 2010, str. 2038-2050)
    Vrsta gradiva - članek, sestavni del
    Leto - 2010
    Jezik - angleški
    COBISS.SI-ID - 4377626
    DOI

vir: FEBS journal. - ISSN 1742-464X (Vol. 277, no. 9, 2010, str. 2038-2050)
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