Variety of antiprion compounds discovered through an in silico screen based on cellular-form prion protein structure: Correlation between antiprion activity and binding affinity.

@article{HosokawaMuto2009VarietyOA,
  title={Variety of antiprion compounds discovered through an in silico screen based on cellular-form prion protein structure: Correlation between antiprion activity and binding affinity.},
  author={Junji Hosokawa-Muto and Yuji O Kamatari and Hironori K. Nakamura and Kazuo Kuwata},
  journal={Antimicrobial agents and chemotherapy},
  year={2009},
  volume={53 2},
  pages={765-71}
}
Transmissible spongiform encephalopathies are associated with the conformational conversion of the prion protein from the cellular form (PrP(C)) to the scrapie form. This process could be disrupted by stabilizing the PrP(C) conformation, using a specific ligand identified as a chemical chaperone. To discover such compounds, we employed an in silico screen that was based on the nuclear magnetic resonance structure of PrP(C). In combination, we performed ex vivo screening using the Fukuoka-1… CONTINUE READING

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