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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
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WRAP_acs%2Ebiochem%2E5b01095.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (1953Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/acs.biochem.5b01095
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 |
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| 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: |
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| 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 | ||||
| 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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