Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

@article{Sato2006InhibitorsOA,
  title={Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.},
  author={Takeshi Sato and P. Kienlen-Campard and Mahiuddin Ahmed and W. Liu and Huilin Li and J. Elliott and S. Aimoto and S. Constantinescu and J. Octave and Steven O. Smith},
  journal={Biochemistry},
  year={2006},
  volume={45 17},
  pages={
          5503-16
        }
}
Amyloid fibrils associated with Alzheimer's disease and a wide range of other neurodegenerative diseases have a cross beta-sheet structure, where main chain hydrogen bonding occurs between beta-strands in the direction of the fibril axis. The surface of the beta-sheet has pronounced ridges and grooves when the individual beta-strands have a parallel orientation and the amino acids are in-register with one another. Here we show that in Abeta amyloid fibrils, Met35 packs against Gly33 in the C… Expand
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