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Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
Department of Chemistry and Department of Physics, University of Warwick, Coventry.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0003-1067-7990
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-6810-1882
Department of Physics, Warwick University, Coventry, Department of Chemistry and Department of Physics, University of Warwick, Coventry.
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Number of Authors: 92016 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 55, no 14, p. 2065-2068Article in journal (Refereed) Published
Abstract [en]

A combined approach, using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) and solid-state NMR (Nuclear Magnetic Resonance), shows a high degree of polymorphism exhibited by Aβ species in forming hydrogen-bonded networks. Two Alzheimer’s Aβ peptides, Ac-Aβ16–22-NH2 and Aβ11–25, selectively labeled with 17O and 15N at specific amino acid residues were investigated. The total amount of peptides labeled with 17O as measured by FTICR-MS enabled the interpretation of dephasing observed in 15N{17O}REAPDOR solid-state NMR experiments. Specifically, about one-third of the Aβ peptides were found to be involved in the formation of a specific >C═17O···H–15N hydrogen bond with their neighbor peptide molecules, and we hypothesize that the rest of the molecules undergo ± n off-registry shifts in their hydrogen bonding networks.

Place, publisher, year, edition, pages
2016. Vol. 55, no 14, p. 2065-2068
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-3009DOI: 10.1021/acs.biochem.5b01095ISI: 000374197100001PubMedID: 26983928Scopus ID: 2-s2.0-84964308549Local ID: 0c14fbe1-4d29-40ed-a247-6aeafe2915c5OAI: oai:DiVA.org:ltu-3009DiVA, id: diva2:975864
Note

Validerad; 2016; Nivå 2; 20160414 (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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