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| Hauptseite > Publikationsdatenbank > Characterization of Mn(II) ion binding to the amyloid-ß peptide in Alzheimer’s disease > print |
| Hauptseite > Publikationsdatenbank > Characterization of Mn(II) ion binding to the amyloid-ß peptide in Alzheimer’s disease > print |
| 001 | 823867 | ||
| 005 | 20210129224856.0 | ||
| 024 | 7 | _ | |a 10.1016/j.jtemb.2016.03.009 |2 doi |
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| 100 | 1 | _ | |a Wallin, C. |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Characterization of Mn(II) ion binding to the amyloid-ß peptide in Alzheimer’s disease |
| 260 | _ | _ | |a München |c 2016 |b Elsevier |
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| 520 | _ | _ | |a Growing evidence links neurodegenerative diseases to metal exposure. Aberrant metal ion concentrationshave been noted in Alzheimer’s disease (AD) brains, yet the role of metals in AD pathogenesis remainsunresolved. A major factor in AD pathogenesis is considered to be aggregation of and amyloid formationby amyloid-ß (Aß) peptides. Previous studies have shown that Aß displays specific binding to Cu(II)and Zn(II) ions, and such binding has been shown to modulate Aß aggregation. Here, we use nuclearmagnetic resonance (NMR) spectroscopy to show that Mn(II) ions also bind to the N-terminal part ofthe Aß(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 molecularmodeling suggest that the weak binding of Mn(II) to Aß may not have a large effect on the peptide’saggregation into amyloid fibrils. However, identification of an additional metal ion displaying Aß bindingreveals more complex AD metal chemistry than has been previously considered in the literature. |
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| 700 | 1 | _ | |a Wärmländer, S. K. T. S. |0 P:(DE-HGF)0 |b 13 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/j.jtemb.2016.03.009 |0 PERI:(DE-600)2174174-8 |p 183-193 |t Journal of trace elements in medicine and biology |v 38 |y 2016 |x 0946-672X |
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