Open AccessQuenched hydrogen-deuterium exchange NMR of a disease-relevant Aβ(1-42) amyloid polymorph
Author(s) -
Marielle Aulikki Wälti,
Julien Orts,
Roland Riek
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0172862
Subject(s) - hydrogen–deuterium exchange , fibril , amyloid fibril , solid state nuclear magnetic resonance , crystallography , chemistry , nuclear magnetic resonance spectroscopy , hydrogen bond , amyloid (mycology) , amyloid β , hydrogen , molecule , nuclear magnetic resonance , stereochemistry , biochemistry , disease , medicine , organic chemistry , physics , pathology , inorganic chemistry
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.