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Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease

Wallin, Cecilia and Kulkarni, Yashraj S. and Abelein, Axel and Jarvet, Jüri and Liao, Qinghua and Strodel, Birgit and Olsson, Lisa and Luo, Jinghui and Abrahams, Jan Pieter and Sholts, Sabrina B. and Roos, Per M. and Kamerlin, Shina C. L. and Gräslund, Astrid and Wärmländer, Sebastian K. T. S.. (2016) Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease. Journal of Trace Elements in Medicine and Biology, 38. pp. 183-193.

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Official URL: http://edoc.unibas.ch/54057/

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Abstract

Growing evidence links neurodegenerative diseases to metal exposure. Aberrant metal ion concentrations have been noted in Alzheimer's disease (AD) brains, yet the role of metals in AD pathogenesis remains unresolved. A major factor in AD pathogenesis is considered to be aggregation of and amyloid formation by amyloid-β (Aβ) peptides. Previous studies have shown that Aβ displays specific binding to Cu(II) and Zn(II) ions, and such binding has been shown to modulate Aβ aggregation. Here, we use nuclear magnetic resonance (NMR) spectroscopy to show that Mn(II) ions also bind to the N-terminal part of the Aβ(1-40) peptide, with a weak binding affinity in the milli- to micromolar range. Circular dichroism (CD) spectroscopy, solid state atomic force microscopy (AFM), fluorescence spectroscopy, and molecular modeling suggest that the weak binding of Mn(II) to Aβ may not have a large effect on the peptide's aggregation into amyloid fibrils. However, identification of an additional metal ion displaying Aβ binding reveals more complex AD metal chemistry than has been previously considered in the literature.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Urban & Fischer
ISSN:0946-672X
e-ISSN:1878-3252
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:26 Oct 2017 15:22
Deposited On:26 Oct 2017 15:22

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