Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer’s β-Amyloid Peptide, and Structural Characterization by Solid State NMR

@inproceedings{Balbach2000AmyloidFF,
  title={Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer’s β-Amyloid Peptide, and Structural Characterization by Solid State NMR},
  author={John J. Balbach and Yoshitaka Ishii and Oleg N Antzutkin and Richard Leapman and Nancy W. Rizzo and Fred Dyda and Jennifer Reed and Robert Tycko},
  year={2000}
}
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22 and representing residues 16 through 22 of the full-length β-amyloid peptide associated with Alzheimer’s disease, is shown by electron microscopy to form highly ordered fibrils upon incubation of aqueous solutions. X-ray powder diffraction and optical birefringence measurements confirm that these are amyloid fibrils. The peptide conformation and supramolecular organization in A β16-22 fibrils are investigated by… CONTINUE READING

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Advances in Magnetic Resonance (Waugh

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