Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph.
Alzheimer's disease is associated with the aggregation into amyloid fibrils of Aβ(1-42) and Aβ(1-40) peptides. Interestingly, these fibrils often do not obtain one single structure but rather show different morphologies, so-called polymorphs. Here, we compare quenched hydrogen-deuterium (H/D) exchange of a disease-relevant Aβ(1-42) fibril for which the 3D structure has been determined by solid-state NMR with H/D exchange previously determined on another structural polymorph. This comparison reveals secondary structural differences between the two polymorphs suggesting that the two polymorphisms can be classified as segmental polymorphs.
Laboratorium für Physikalische Chemie, ETH Zürich, Zürich, Switzerland.
Marielle Aulikki
MA
Wälti
Laboratorium für Physikalische Chemie, ETH Zürich, Zürich, Switzerland.
Julien
J
Orts
Laboratorium für Physikalische Chemie, ETH Zürich, Zürich, Switzerland.
Roland
R
Riek
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D041961:Deuterium Exchange Measurement; D017666:Deuterium Oxide / Q000737:chemistry; D004121:Dimethyl Sulfoxide / Q000737:chemistry; D004926:Escherichia coli; D007700:Kinetics; D008854:Microscopy, Electron; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D012997:Solvents; C075222:amyloid beta-protein (1-42); D017666:Deuterium Oxide; D004121:Dimethyl Sulfoxide