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Structure and texture of fibrous crystals formed by Alzheimer's abeta(11-25) peptide fragment.
- Source :
-
Structure (London, England : 1993) [Structure] 2003 Aug; Vol. 11 (8), pp. 915-26. - Publication Year :
- 2003
-
Abstract
- Amyloid fibril deposition is central to the pathology of Alzheimer's disease. X-ray diffraction from amyloid fibrils formed from full-length Abeta(1-40) and from a shorter fragment, Abeta(11-25), have revealed cross-beta diffraction fingerprints. Magnetic alignment of Abeta(11-25) amyloid fibrils gave a distinctive X-ray diffraction texture, allowing interpretation of the diffraction data and a model of the arrangement of the peptides within the amyloid fiber specimen to be constructed. An intriguing feature of the structure of fibrillar Abeta(11-25) is that the beta sheets, of width 5.2 nm, stack by slipping relative to each other by the length of two amino acid units (0.70 nm) to form beta ribbons 4.42 nm in thickness. Abeta(1-40) amyloid fibrils likely consist of once-folded hairpins, consistent with the size of the fibers obtained using electron microscopy and X-ray diffraction.
- Subjects :
- Alzheimer Disease pathology
Amino Acid Sequence
Amyloid beta-Peptides ultrastructure
Computer Simulation
Humans
Magnetics
Models, Chemical
Models, Molecular
Peptide Fragments chemical synthesis
Protein Structure, Secondary
Protein Structure, Tertiary
Alzheimer Disease metabolism
Amyloid beta-Peptides chemistry
Crystallography, X-Ray
Peptide Fragments chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0969-2126
- Volume :
- 11
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Structure (London, England : 1993)
- Publication Type :
- Academic Journal
- Accession number :
- 12906823
- Full Text :
- https://doi.org/10.1016/s0969-2126(03)00149-7