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@ARTICLE{Wallin:823867,
      author       = {Wallin, C. and Kulkarni, Y. S. and Abelein, A and Jarvet,
                      J. and Liao, Qinghua and Strodel, Birgit and Olsson, L. and
                      Luo, J. and Abrahams, J. P. and Sholts, S. B. and Roos, P.
                      M. and Kamerlin, S. C. L. and Gräslund, A. and
                      Wärmländer, S. K. T. S.},
      title        = {{C}haracterization of {M}n({II}) ion binding to the
                      amyloid-ß peptide in {A}lzheimer’s disease},
      journal      = {Journal of trace elements in medicine and biology},
      volume       = {38},
      issn         = {0946-672X},
      address      = {München},
      publisher    = {Elsevier},
      reportid     = {FZJ-2016-06507},
      pages        = {183-193},
      year         = {2016},
      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.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000385473600023},
      pubmed       = {pmid:27085215},
      doi          = {10.1016/j.jtemb.2016.03.009},
      url          = {https://juser.fz-juelich.de/record/823867},
}