Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils

@article{Ahmed2010StructuralCO,
  title={Structural conversion of neurotoxic amyloid-$\beta$(1–42) oligomers to fibrils},
  author={Mahiuddin Ahmed and Judianne Davis and Darryl Aucoin and Takeshi Sato and S. Ahuja and S. Aimoto and J. Elliott and W. V. Van Nostrand and Steven O. Smith},
  journal={Nature structural \& molecular biology},
  year={2010},
  volume={17},
  pages={561 - 567}
}
The amyloid-β1–42 (Aβ42) peptide rapidly aggregates to form oligomers, protofibils and fibrils en route to the deposition of amyloid plaques associated with Alzheimer's disease. We show that low-temperature and low-salt conditions can stabilize disc-shaped oligomers (pentamers) that are substantially more toxic to mouse cortical neurons than protofibrils and fibrils. We find that these neurotoxic oligomers do not have the β-sheet structure characteristic of fibrils. Rather, the oligomers are… Expand
Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils.
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Polymorphic Structures of Alzheimer ' s Beta-amyloid Globulomers
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