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Supramolecular structural constraints on Alzheimer's β-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-1067-7990
Division of Physical Science, Office of Research Services, National Institutes of Health, Bethesda.
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda.
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda.
2002 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 41, no 51, p. 15436-15450Article in journal (Refereed) Published
Abstract [en]

We describe electron microscopy (EM), scanning transmission electron microscopy (STEM), and solid-state nuclear magnetic resonance (NMR) measurements on amyloid fibrils formed by the 42-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1-42) and by residues 10-35 of the full-length peptide (Aβ10-35). These measurements place constraints on the supramolecular structure of the amyloid fibrils, especially the type of β-sheets present in the characteristic amyloid cross-β structural motif and the assembly of these β-sheets into a fibril. EM images of negatively stained Aβ10-35 fibrils and measurements of fibril mass per length (MPL) by STEM show a strong dependence of fibril morphology and MPL on pH. Aβ10-35 fibrils formed at pH 3.7 are single "protofilaments" with MPL equal to twice the value expected for a single cross-β layer. Aβ10-35 fibrils formed at pH 7.4 are apparently pairs of protofilaments or higher order bundles. EM and STEM data for Aβ1-42 fibrils indicate that protofilaments with MPL equal to twice the value expected for a single cross-β layer are also formed by Aβ1-42 and that these protofilaments exist singly and in pairs at pH 7.4. Solid-state NMR measurements of intermolecular distances in Aβ10-35 fibrils, using multiple-quantum 13C NMR, 13C-13C dipolar recoupling, and 15N-13C dipolar recoupling techniques, support the in-register parallel β-sheet organization previously established by Lynn, Meredith, Botto, and co-workers [Benzinger et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 13407-13412; Benzinger et al. (2000) Biochemistry 39, 3491-3499] and show that this β-sheet organization is present at pH 3.7 as well as pH 7.4 despite the differences in fibril morphology and MPL. Solid-state NMR measurements of intermolecular distances in Aβ1-42 fibrils, which represent the first NMR data on Aβ1-42 fibrils, also indicate an in-register parallel β-sheet organization. These results, along with previously reported data on Aβ1-40 fibrils, suggest that the supramolecular structures of Aβ10-35, Aβ1-40, and Aβ1-42 fibrils are quite similar. A schematic structural model of these fibrils, consistent with known experimental EM, STEM, and solid-state NMR data, is presented

Place, publisher, year, edition, pages
2002. Vol. 41, no 51, p. 15436-15450
Keywords [en]
Technology - Chemical engineering
Keywords [sv]
Teknikvetenskap - Kemiteknik
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-12447DOI: 10.1021/bi0204185ISI: 000180015100040Scopus ID: 2-s2.0-0037168446Local ID: b98eb380-b331-11de-b4d6-000ea68e967bOAI: oai:DiVA.org:ltu-12447DiVA, id: diva2:985398
Note
Validerad; 2002; 20091007 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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