Journal Article

FZJ-2016-06507

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Characterization of Mn(II) ion binding to the amyloid-ß peptide in Alzheimer’s disease

Wallin, C. ; Kulkarni, Y. S. ; Abelein, A. ; Jarvet, J. ; Liao, Q. ; Strodel, B.FZJ* ; Olsson, L. ; Luo, J. ; Abrahams, J. P. ; Sholts, S. B. ; Roos, P. M. ; Kamerlin, S. C. L. ; Gräslund, A. ; Wärmländer, S. K. T. S. (Corresponding author)

2016
Elsevier München

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Please use a persistent id in citations: doi:10.1016/j.jtemb.2016.03.009

Abstract: 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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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)

Appears in the scientific report 2016

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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