Designing drugs to stop the formation of prion aggregates and other amyloids

Joanna Masel, Vincent A.A. Jansen

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Amyloid protein aggregates are implicated in many neurodegenerative diseases, including Alzheimer's disease and the prion diseases. Therapeutics to block amyloid formation are often tested in vitro, but it is not clear how to extrapolate from these experiments to a clinical setting, where the effective drug dose may be much lower. Here we address this question using a theoretical kinetic model to calculate the growth rate of protein aggregates as a function of the dose of each of three categories of drug. We find that therapeutics which block the growing ends of amyloids are the most promising, as alternative strategies may be ineffective or even accelerate amyloid formation at low drug concentrations. Our mathematical model can be used to identify and optimise an end-blocking drug in vitro. Our model also suggests an alternative explanation for data previously thought to prove the existence of an entity known as protein X. (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)47-59
Number of pages13
JournalBiophysical Chemistry
Issue number1-3
StatePublished - Dec 15 2000
Externally publishedYes


  • Alzheimer's disease
  • Amyloid formation
  • Mathematical model
  • Prion disease
  • Replication mechanism
  • Therapeutics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry


Dive into the research topics of 'Designing drugs to stop the formation of prion aggregates and other amyloids'. Together they form a unique fingerprint.

Cite this