Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.

ABSTRACT: Water is essential for protein folding and assembly of amyloid fibrils. Internal water cavities have been proposed for several amyloid fibrils, but no direct structural and dynamical data have been reported on the water dynamics and site-specific interactions of water with the fibrils. Here we use solid-state NMR spectroscopy to investigate the water interactions of several Aβ40 fibrils. ¹H spectral lineshapes, T₂ relaxation times, and two-dimensional (2D) ¹H-¹³C correlation spectra show that there are five distinct water pools: three are peptide-bound water, while two are highly dynamic water that can be assigned to interfibrillar water and bulk-like matrix water. All these water pools are associated with the fibrils on the nanometer scale. Wate

SUBMITTER: Wang T 

PROVIDER: S-EPMC5808936 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature