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Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR
| Content Provider | Semantic Scholar |
|---|---|
| Author | Balbach, John J. Ishii, Yoshitaka Antzutkin, Oleg N. Leapman, Richard D. Rizzo, Nancy W. Dyda, Fred Reed, Jennifer Tycko, Robert |
| Copyright Year | 2000 |
| Abstract | The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH2, called Aβ16-22 and representing residues 16−22 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 Aβ16-22 fibrils are investigated by solid state 13C NMR measurements. Two-dimensional magic-angle spinning (2D MAS) exchange and constant-time double-quantum-filtered dipolar recoupling (CTDQFD) measurements indicate a β-strand conformation of the peptide backbone at the central phenylalanine. One-dimensional and two-dimensional spectra of selectively and uniformly labeled samples exhibit 13C NMR line widths of <2 ppm, demonstrating that the peptide, including amino acid side chains, has a well-ordered conformation in the fibrils. Two-dimensional 13C−13C chemi... |
| Starting Page | 13748 |
| Ending Page | 13759 |
| Page Count | 12 |
| File Format | PDF HTM / HTML |
| DOI | 10.1021/bi0011330 |
| Alternate Webpage(s) | http://www2.chem.uic.edu/ishii/group/publications/pub_pdf/2000_JMB_Ab16-22.pdf |
| Alternate Webpage(s) | http://www.chem.uic.edu/ishii/group/publications/pub_pdf/2000_JMB_Ab16-22.pdf |
| Alternate Webpage(s) | https://doi.org/10.1021/bi0011330 |
| Volume Number | 39 |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
