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A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Open accessAbstract
We present a structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ 1–40 ), based on a set of experimental constraints from solid state NMR spectroscopy. The model additionally incorporates the cross-β structural motif established by x-ray fiber diffraction and satisfies constraints on Aβ 1–40 fibril dimensions and mass-per-length determined from electron microscopy. Approximately the first 10 residues of Aβ 1–40 are structurally disordered in the fibrils. Residues 12–24 and 30–40 adopt β-strand conformations and form parallel β-sheets through intermolecular hydrogen bonding. Residues 25–29 contain a bend of the peptide backbone that brings the two β-sheets in contact through sidechain-sidechain interactions. A single cross-β unit is then a double-layered β-sheet structure with a hydrophobic core and one hydrophobic face. The only charged sidechains in the core are those of D23 and K28, which form salt bridges. Fibrils with minimum mass-per-length and diameter consist of two cross-β units with their hydrophobic faces juxtaposed.
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Metadata
- Authors
- Petkova, A. T., Ishii, Y., Balbach, J. J., Antzutkin, O. N., Leapman, R. D., Delaglio, F., & Tycko, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-12-12
- Volume
- 99
- Issue
- 26
- Pages
- 16742-16747
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2067214887
- Cited by
- 1,845
- References
- 3
- FWCI
- 36.19
- Type
- journal article
- Language
- en
- Open access
- green
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