Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus.

ABSTRACT: We investigate the variability in the dynamics of the disordered N-terminal domain of amyloid-β fibrils (Aβ), comprising residues 1-16 of Aβ_1-40, due to post-translational modifications and mutations in the β-bend regions known to modulate aggregation properties. Using ²H static solid-state NMR approaches, we compare the dynamics in the wild-type Aβ fibrils in the threefold symmetric polymorph with the fibrils from three post-translational modification sequences: isoaspartate-D7, the phosphorylation of S8, and an N-terminal truncation ΔE3. Additional comparisons are made with the mutants in the β-bend region (residues 21-23) corresponding to the familial Osaka E22Δ deletion and D23N Iowa mutation. We also include the aggregates induced by Zn²⁺ ions. The dyn

SUBMITTER: Vugmeyster L 

PROVIDER: S-EPMC6817547 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature