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@ARTICLE{Zhang:843873,
      author       = {Zhang, Tao and Pauly, Thomas and Nagel-Steger, Luitgard},
      title        = {{S}toichiometric {Z}n 2+ interferes with the
                      self-association of {A}β42: {I}nsights from size
                      distribution analysis},
      journal      = {International journal of biological macromolecules},
      volume       = {113},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2018-01403},
      pages        = {631-639},
      year         = {2018},
      abstract     = {The abnormal aggregation of amyloid β (Aβ) peptides in
                      the brain has been recognized as a central event in
                      Alzheimer's disease (AD). Divalent metal ions such as Zn2+
                      have been shown to be closely involved in modulating Aβ
                      self-association. Although the link between Zn2+
                      dyshomeostasis and brain Aβ deposition has been
                      established, the effect of Zn2+ on the aggregation of Aβ is
                      still incompletely clarified. By combining analytical
                      ultracentrifugation (AUC), circular dichroism (CD)
                      spectroscopy, thioflavin T (ThT) assay and atomic force
                      microscopy (AFM) imaging, we analyzed the impact of
                      stoichiometric Zn2+ on the aggregation process of Aβ42, the
                      main toxic isoform of Aβ species in the brain. Aβ42
                      aggregates found in the presence of Zn2+ were smaller in
                      size, non-fibrillary and showed less β-sheet structures
                      than aggregates formed in absence of Zn2+. AUC showed that
                      Zn2+ was capable of retaining monomeric Aβ42 in solution.
                      Zn2+ chelation by EDTA totally reversed the inhibitory
                      effect of Zn2+ on Aβ42 fibrillation. Our results provide
                      further evidence that Zn2+ shifts the self-association of
                      Aβ42 toward a non-fibrillary pathway by interfering with
                      the aggregation process at multiple levels.},
      cin          = {ICS-6},
      ddc          = {540},
      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},
      pubmed       = {pmid:29476859},
      UT           = {WOS:000432503100074},
      doi          = {10.1016/j.ijbiomac.2018.02.123},
      url          = {https://juser.fz-juelich.de/record/843873},
}