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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The importance of the disulfide bond in prion protein conversion.

The conversion of normal, protease sensitive prion protein (PrP-sen) to the abnormal protease-resistant form (PrP-res) is of central importance in the pathogenesis of scrapie and other transmissible spongiform encephalopathies. In the present study, the effects of reduction of the disulfide bond on the PrP-sen to PrP-res conversion in a cell-free system were examined. The addition of the disulfide reducing agent dithiothreitol inhibited the cell-free conversion reaction with an IC50 of 2-2.5 mM. Separate pretreatment of either PrP-sen or PrP-res with dithiothreitol and an alkylating agent also inhibited the conversion reaction. Results of this study show that preservation of the disulfide bond is important in the conversion of PrP-sen to PrP-res.[1]

References

  1. The importance of the disulfide bond in prion protein conversion. Herrmann, L.M., Caughey, B. Neuroreport (1998) [Pubmed]
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