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Amyloid hydrogen bonding polymorphism evaluated by15N{17O}REAPDOR solid-state NMR and ultra-high resolution fourier transform ion cyclotron resonance mass spectrometry

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Wei, Juan, Antzutkin, Oleg N., Filippov, Andrei V., Iuga, Dinu, Lam, Pui Yiu, Barrow, Mark P., Dupree, Ray, Brown, Steven P. and O’Connor, Peter B. (2016) Amyloid hydrogen bonding polymorphism evaluated by15N{17O}REAPDOR solid-state NMR and ultra-high resolution fourier transform ion cyclotron resonance mass spectrometry. Biochemistry, 55 (14). pp. 2065-2068. doi:10.1021/acs.biochem.5b01095 ISSN 0006-2960.

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Official URL: http://dx.doi.org/10.1021/acs.biochem.5b01095

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Abstract

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.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Science > Physics
Library of Congress Subject Headings (LCSH): Amyloid, Mass spectrometry
Journal or Publication Title: Biochemistry
Publisher: American Chemical Society
ISSN: 0006-2960
Official Date: 17 March 2016
Dates:
DateEvent
17 March 2016Published
Volume: 55
Number: 14
Number of Pages: 4
Page Range: pp. 2065-2068
DOI: 10.1021/acs.biochem.5b01095
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 23 June 2016
Date of first compliant Open Access: 23 June 2016
Funder: Engineering and Physical Sciences Research Council (EPSRC), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Birmingham Science City, Advantage West Midlands (AWM), European Regional Development Fund (ERDF)
Grant number: EP/J000302/1 (EPSRC), EP/F017901/1 (EPSRC)

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