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Hydrogen bonding in Alzheimer’s amyloid-β fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-1067-7990
Department of Physics, Warwick University, Coventry.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0002-6810-1882
Department of Physics, Warwick University, Coventry.
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2012 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 51, no 41, p. 10289-10292Article in journal (Refereed) Published
Abstract [en]

An exclusive label: 15N{17O} REAPDOR NMR was used to validate intermolecular C17O⋅⋅⋅H15N hydrogen bonding in Ac-Aβ(16–22)-NH2 (see scheme) and Aβ(11–25) amyloid fibrils, which are associated with Alzheimer’s disease, by selectively labeling them with 17O and 15N. This method was effective for confirming the structure of these fibrils, and could be useful for a number of other biological samples.

Place, publisher, year, edition, pages
2012. Vol. 51, no 41, p. 10289-10292
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-5762DOI: 10.1002/anie.201203595ISI: 000309406900014Scopus ID: 2-s2.0-84867049078Local ID: 3f1639c6-f7b8-4640-8df0-a6b4d645051fOAI: oai:DiVA.org:ltu-5762DiVA, id: diva2:978637
Note
Validerad; 2012; 20120918 (andbra)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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Antzutkin, OlegFilippov, Andrei

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