Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid β Assemblies.

ABSTRACT: Alzheimer's disease is the most fatal neurodegenerative disorder characterized by the aggregation and deposition of Amyloid β (Aβ) oligomers in the brain of patients. Two principal variants of Aβ exist in humans: Aβ_1-40 and Aβ_1-42. The former is the most abundant in the plaques, while the latter is the most toxic species and forms fibrils more rapidly. Interestingly, fibrils of Aβ_1-40 peptides can only assume U-shaped conformations while Aβ_1-42 can also arrange as S-shaped three-stranded chains, as recently discovered. As alterations in protein conformational arrangement correlate with cell toxicity and speed of disease progression, it is important to characterize, at molecular level, the conformational dynamics of amyloid fibrils. In this work,

SUBMITTER: Grasso G 

PROVIDER: S-EPMC5855793 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature