A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
National Institutes of Health · Luleå University of Technology · +2 more institutions
Abstract
We present a structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on a set of experimental constraints from solid state NMR spectroscopy. The model additionally incorporates the cross-beta structural motif established by x-ray fiber diffraction and satisfies constraints on Abeta(1-40) fibril dimensions and mass-per-length determined from electron microscopy. Approximately the first 10 residues of Abeta(1-40) are structurally disordered in the fibrils. Residues 12-24 and 30-40 adopt beta-strand conformations and form parallel beta-sheets through intermolecular hydrogen bonding. Residues 25-29 contain a bend of the peptide…
Citation impact
- FWCI
- 37.13
- Percentile
- 100%
- References
- 52
Authors
7- ATAneta T. PetkovaCorresponding
National Institutes of Health, Luleå University of Technology, National Institute of Diabetes and Digestive and Kidney Diseases, Office of Research Services
- YIYoshitaka Ishii
National Institutes of Health, Luleå University of Technology, National Institute of Diabetes and Digestive and Kidney Diseases, Office of Research Services
- JJJohn J. Balbach
National Institutes of Health, Luleå University of Technology, National Institute of Diabetes and Digestive and Kidney Diseases, Office of Research Services
- ONOleg N. Antzutkin
National Institutes of Health, Luleå University of Technology, National Institute of Diabetes and Digestive and Kidney Diseases, Office of Research Services
- RDRichard D. Leapman
National Institutes of Health, Luleå University of Technology, National Institute of Diabetes and Digestive and Kidney Diseases, Office of Research Services
Topics & keywords
- Fibril
- Chemistry
- Crystallography
- Peptide
- Beta sheet
- Fiber diffraction
- Solid-state nuclear magnetic resonance
- Amyloid (mycology)