Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.

ABSTRACT: Amyloid-β (Aβ) peptide is the major component of plaques found in Alzheimer's disease patients. Using solid-state ²H NMR relaxation performed on selectively deuterated methyl groups, we probed the dynamics in the threefold symmetric and twofold symmetric polymorphs of native Aβ as well as the protofibrils of the D23N mutant. Specifically, we investigated the methyl groups of two leucine residues that belong to the hydrophobic core (L17 and L34) as well as M35 residues belonging to the hydrophobic interface between the cross-β subunits, which has been previously found to be water-accessible. Relaxation measurements performed over 310-140 K and two magnetic field strengths provide insights into conformational variability within and between polymorphs. Core packing variations withi

SUBMITTER: Vugmeyster L 

PROVIDER: S-EPMC5113154 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature