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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
National Institutes of Health.
National Institutes of Health.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-1067-7990
National Institutes of Health.
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2000 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 39, no 45, p. 13748-13759Article in journal (Refereed) Published
Abstract [en]

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 chemical shift correlation spectroscopy permits a nearly complete assignment of backbone and side chain 13C NMR signals and indicates that the β-strand conformation extends across the entire hydrophobic segment from Leu17 through Ala21. 13C multiple-quantum (MQ) NMR and 13C/15N rotational echo double-resonance (REDOR) measurements indicate an antiparallel organization of β-sheets in the Aβ16-22 fibrils. These results suggest that the degree of structural order at the molecular level in amyloid fibrils can approach that in peptide or protein crystals, suggest how the supramolecular organization of β-sheets in amyloid fibrils can be dependent on the peptide sequence, and illustrate the utility of solid state NMR measurements as probes of the molecular structure of amyloid fibrils. Aβ16-22 is among the shortest fibril-forming fragments of full-length β-amyloid reported to date, and hence serves as a useful model system for physical studies of amyloid fibril formation.

Place, publisher, year, edition, pages
2000. Vol. 39, no 45, p. 13748-13759
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-4358DOI: 10.1021/bi0011330ISI: 000165412800015Scopus ID: 2-s2.0-0034649352Local ID: 24c110a0-bc11-11db-a46c-000ea68e967bOAI: oai:DiVA.org:ltu-4358DiVA, id: diva2:977223
Note
Validerad; 2000; 20070214 (bajo)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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Antzutkin, Oleg

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