The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology.

@article{Seilheimer1997TheTO,
  title={The toxicity of the Alzheimer's beta-amyloid peptide correlates with a distinct fiber morphology.},
  author={Bernd Seilheimer and Bernd Bohrmann and Luca Bondolfi and Friedemann Mueller and Dietrich Stueber and Heinz D{\"o}beli},
  journal={Journal of structural biology},
  year={1997},
  volume={119 1},
  pages={59-71}
}
In an attempt to elucidate the relationship among aggregation properties, fiber morphology, and cellular toxicity several beta-amyloid peptides (A beta) were prepared according to a standardized procedure. Peptides either carried mutations inside the membrane anchor segment around amino acid position 35 or their carboxy terminus was shortened from 42 to 41, 40, or 39 amino acids. The time-dependent self-assembly of monomeric A beta into fibers was simultaneously monitored by electron microscopy… CONTINUE READING