Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass SpectrometryShow others and affiliations
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
Identifiers
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)
2016-09-292016-09-292023-09-05Bibliographically approved