Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics

  title={Prevention of Transthyretin Amyloid Disease by Changing Protein Misfolding Energetics},
  author={P. Hammarstr{\"o}m and R. Wiseman and E. Powers and J. Kelly},
  pages={713 - 716}
  • P. Hammarström, R. Wiseman, +1 author J. Kelly
  • Published 2003
  • Chemistry, Medicine
  • Science
  • Genetic evidence suggests that inhibition of amyloid fibril formation by small molecules should be effective against amyloid diseases. Known amyloid inhibitors appear to function by shifting the aggregation equilibrium away from the amyloid state. Here, we describe a series of transthyretin amyloidosis inhibitors that functioned by increasing the kinetic barrier associated with misfolding, preventing amyloidogenesis by stabilizing the native state. The trans-suppressor mutation, threonine 119… CONTINUE READING
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