Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates.

@article{Margalith2012PolythiophenesIP,
  title={Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates.},
  author={Ilan Margalith and Carlo Suter and Boris A Ballmer and Petra Schwarz and Cinzia Tiberi and Tiziana Sonati and Jeppe Falsig and Sofie Nystr{\"o}m and Per Hammarstr{\"o}m and Andreas KO {\AA}slund and K Peter R Nilsson and Alice Yen-Wen Yam and Eric Whitters and Simone Hornemann and Adriano Aguzzi},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 23},
  pages={18872-87}
}
Luminescent conjugated polymers (LCPs) interact with ordered protein aggregates and sensitively detect amyloids of many different proteins, suggesting that they may possess antiprion properties. Here, we show that a variety of anionic, cationic, and zwitterionic LCPs reduced the infectivity of prion-containing brain homogenates and of prion-infected cerebellar organotypic cultured slices and decreased the amount of scrapie isoform of PrP(C) (PrP(Sc)) oligomers that could be captured in an… CONTINUE READING
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