Amyloid Hydrogen Bonding Polymorphism Evaluated by 15N{17O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry | Zendy

Juan Wei | Zendy; Oleg N. Antzutkin | Zendy; Andrei Filippov | Zendy; Dinu Iuga | Zendy; Yuko P. Y. Lam | Zendy; Mark P. Barrow | Zendy; R. Dupree | Zendy; Steven P. Brown | Zendy; Peter B. O’Connor | Zendy

Open Access

Amyloid Hydrogen Bonding Polymorphism Evaluated by ¹⁵N{¹⁷O}REAPDOR Solid-State NMR and Ultra-High Resolution Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Author(s) -

Juan Wei,

Oleg N. Antzutkin,

Andrei Filippov,

Dinu Iuga,

Yuko P. Y. Lam,

Mark P. Barrow,

R. Dupree,

Steven P. Brown,

Peter B. O’Connor

Publication year - 2016

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/acs.biochem.5b01095

Subject(s) - fourier transform ion cyclotron resonance , mass spectrometry , solid state nuclear magnetic resonance , ion , chemistry , high resolution , ion cyclotron resonance , solid state , nuclear magnetic resonance , fourier transform , analytical chemistry (journal) , hydrogen bond , cyclotron , physics , molecule , chromatography , remote sensing , quantum mechanics , geology , organic chemistry

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.

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