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@ARTICLE{Strodel:872769,
      author       = {Strodel, Birgit and Coskuner-Weber, Orkid},
      title        = {{T}ransition {M}etal {I}on {I}nteractions with {D}isordered
                      {A}myloid-β {P}eptides in the {P}athogenesis of
                      {A}lzheimer’s {D}isease: {I}nsights from {C}omputational
                      {C}hemistry {S}tudies},
      journal      = {Journal of chemical information and modeling},
      volume       = {59},
      number       = {5},
      issn         = {1549-960X},
      address      = {Washington, DC},
      publisher    = {American Chemical Society64160},
      reportid     = {FZJ-2020-00247},
      pages        = {1782 - 1805},
      year         = {2019},
      abstract     = {Monomers and oligomers of the amyloid-β peptide aggregate
                      to form the fibrils found in the brains of Alzheimer’s
                      disease patients. These monomers and oligomers are largely
                      disordered and can interact with transition metal ions,
                      affecting the mechanism and kinetics of amyloid-β
                      aggregation. Due to the disordered nature of amyloid-β, its
                      rapid aggregation, as well as solvent and paramagnetic
                      effects, experimental studies face challenges in the
                      characterization of transition metal ions bound to
                      amyloid-β monomers and oligomers. The details of the
                      coordination chemistry between transition metals and
                      amyloid-β obtained from experiments remain debated.
                      Furthermore, the impact of transition metal ion binding on
                      the monomeric or oligomeric amyloid-β structures and
                      dynamics are still poorly understood. Computational
                      chemistry studies can serve as an important complement to
                      experimental studies and can provide additional knowledge on
                      the binding between amyloid-β and transition metal ions.
                      Many research groups conducted first-principles
                      calculations, ab initio molecular dynamics simulations,
                      quantum mechanics/classical mechanics simulations, and
                      classical molecular dynamics simulations for studying the
                      interplay between transition metal ions and amyloid-β
                      monomers and oligomers. This review summarizes the current
                      understanding of transition metal interactions with
                      amyloid-β obtained from computational chemistry studies. We
                      also emphasize the current view of the coordination
                      chemistry between transition metal ions and amyloid-β. This
                      information represents an important foundation for future
                      metal ion chelator and drug design studies aiming to combat
                      Alzheimer’s disease.},
      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:30933519},
      UT           = {WOS:000469884900011},
      doi          = {10.1021/acs.jcim.8b00983},
      url          = {https://juser.fz-juelich.de/record/872769},
}