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.
Biochemistry
; 55(14): 2065-8, 2016 Apr 12.
Article
em En
| MEDLINE
| ID: mdl-26983928
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 Aß species in forming hydrogen-bonded networks. Two Alzheimer's Aß peptides, Ac-Aß(16-22)-NH2 and Aß(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 Aß peptides were found to be involved in the formation of a specific >Câ(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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Modelos Moleculares
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Peptídeos beta-Amiloides
/
Amiloide
Limite:
Humans
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article