Potent inhibition of scrapie-associated PrP accumulation by congo red

J Neurochem. 1992 Aug;59(2):768-71. doi: 10.1111/j.1471-4159.1992.tb09437.x.


Transmissible spongiform encephalopathies (prion diseases), Alzheimer's disease, and other amyloidoses result in the accumulation of certain abnormally stable proteins that are thought by many to play central roles in disease pathogenesis. Using scrapie-infected neuroblastoma cells as a model system, we found that Congo red, an amyloid-binding dye, potently inhibits the accumulation of the scrapie-associated, protease-resistant isoform of protein PrP without affecting the metabolism of the normal isoform. Growth of the cells with submicromolar concentrations of Congo red for 5 days reduced the amount of protease-resistant PrP detected in the cultures by greater than 90%. This activity of Congo red suggests that it selectively disrupts the conversion of PrP to the protease-resistant isoform or destabilizes this isoform once it is made. Potential therapeutic applications of Congo red are discussed.

MeSH terms

  • Animals
  • Congo Red / pharmacology*
  • Immunoblotting
  • Isomerism
  • Mice
  • Neuroblastoma / metabolism
  • Neuroblastoma / pathology
  • PrPSc Proteins
  • Prions / antagonists & inhibitors
  • Prions / chemistry
  • Prions / metabolism*
  • Tumor Cells, Cultured / drug effects
  • Tumor Cells, Cultured / metabolism
  • Tumor Cells, Cultured / pathology


  • PrPSc Proteins
  • Prions
  • Congo Red