title: Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP.
abstract: Dynamic Nuclear Polarization solid-state NMR holds the potential to enable a dramatic increase in sensitivity by exploiting the large magnetic moment of the electron. However, applications to biological solids are hampered in uniformly isotopically enriched biomacromolecules due to line broadening which yields a limited spectral resolution at cryogenic temperatures. We show here that high magnetic fields allow to overcome the broadening of resonance lines often experienced at liquid nitrogen temperatures. For a fibril sample of the Alzheimer's disease β-amyloid peptide, we find similar line widths at low temperature and at room temperature. The presented results open new perspectives for structural investigations in the solid-state.
authors.affiliation: Helmholtz-Zentrum München (HMGU), Deutsches Forschungszentrum für Gesundheit und Umwelt, Ingolstädter Landstr. 1, 85764 Neuherberg, Germany.
authors.forename: Juan-Miguel
authors.initials: JM
authors.lastname: Lopez del Amo
authors.forename: Dennis
authors.initials: D
authors.lastname: Schneider
authors.forename: Antoine
authors.initials: A
authors.lastname: Loquet
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure; D003080:Cold Temperature; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D016229:Amyloid beta-Peptides