Modeling the Co²⁺Binding to Amyloid Peptide Aβ13–23 in Water Environment by NMR Spectroscopy

Abstract

© 2017, Springer Science+Business Media, LLC, part of Springer Nature. Alzheimer’s disease is a fatal neurodegenerative disorder involving the abnormal accumulation and deposition of peptides (amyloid-β, Aβ) derived from the amyloid precursor protein. Various factors that cause pathology data are revealed, but, at the moment, there is no clear understanding of the processes of plaque formation. This is interesting and actual problem because metals such as zinc, manganese, and others induce Aβ aggregation and fibril formation at high metal concentrations, while low concentration metal ions selectively destabilize the Aβ oligomeric species. In present paper, we report a structural studies of the Co2+ion binding sites of Aβ fragments in water environment by 1D (1H) and 2D (1H-1H) NMR spectroscopy. According to the observed changes in the NMR spectra that were determined, the cobalt binding center of the Aβ13–23peptide is associated with the aspartate and glutamine residues. Structural model of cobalt associated with Aβ peptide was obtained.