title: Amyloid Hydrogen Bonding Polymorphism Evaluated by (15)N{(17)O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.
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-Aβ(16-22)-NH2 and Aβ(11-25), selectively labeled with (17)O and (15)N at specific amino acid residues were investigated. The total amount of peptides labeled with (17)O as measured by FTICR-MS enabled the interpretation of dephasing observed in (15)N{(17)O}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═(17)O···H-(15)N 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.
authors.forename: Juan
authors.initials: J
authors.lastname: Wei
authors.affiliation: Chemistry of Interfaces, Luleå University of Technology , SE-971 87, Luleå, Sweden.
authors.forename: Oleg N
authors.initials: ON
authors.lastname: Antzutkin
authors.affiliation: Chemistry of Interfaces, Luleå University of Technology , SE-971 87, Luleå, Sweden.
authors.forename: Andrei V
authors.initials: AV
authors.lastname: Filippov
authors.forename: Dinu
authors.initials: D
authors.lastname: Iuga
authors.forename: Pui Yiu
authors.initials: PY
authors.lastname: Lam
authors.forename: Mark P
authors.initials: MP
authors.lastname: Barrow
authors.forename: Ray
authors.initials: R
authors.lastname: Dupree
authors.forename: Steven P
authors.initials: SP
authors.lastname: Brown
authors.forename: Peter B
authors.initials: PB
authors.lastname: O'Connor
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D017357:Cyclotrons; D005583:Fourier Analysis; D006801:Humans; D006860:Hydrogen Bonding; D007553:Isotope Labeling; D013058:Mass Spectrometry; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D010103:Oxygen Isotopes; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D055550:Protein Stability; D053719:Tandem Mass Spectrometry
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D009587:Nitrogen Isotopes; D009842:Oligopeptides; D010103:Oxygen Isotopes; D010446:Peptide Fragments; C410220:amyloid beta-protein (11-25); C417223:amyloid beta-protein (16-22)