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@ARTICLE{Nedaei:996128,
      author       = {Nedaei, Hadi and Rezaei-Ghaleh, Nasrollah and Giller, Karin
                      and Becker, Stefan and Karami, Leila and Moosavi-Movahedi,
                      Ali Akbar and Griesinger, Christian and Saboury, Ali Akbar},
      title        = {{T}he calcium-free form of atorvastatin inhibits
                      amyloid-β(1–42) aggregation in vitro},
      journal      = {The journal of biological chemistry},
      volume       = {298},
      number       = {3},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2023-01125},
      pages        = {101662 -},
      year         = {2022},
      abstract     = {Alzheimer's disease is characterized by the presence of
                      extraneuronal amyloid plaques composed of amyloid-beta (Aβ)
                      fibrillar aggregates in the brains of patients. In mouse
                      models, it has previously been shown that atorvastatin
                      (Ator), a cholesterol-lowering drug, has some reducing
                      effect on the production of cerebral Aβ. A meta-analysis on
                      humans showed moderate effects in the short term but no
                      improvement in the Alzheimer's Disease Assessment
                      Scale—Cognitive Subscale behavioral test. Here, we explore
                      a potential direct effect of Ator on Aβ42 aggregation.
                      Using NMR-based monomer consumption assays and CD
                      spectroscopy, we observed a promoting effect of Ator in its
                      original form (Ator-calcium) on Aβ42 aggregation, as
                      expected because of the presence of calcium ions. The effect
                      was reversed when applying a CaCO3-based calcium ion
                      scavenging method, which was validated by the aforementioned
                      methods as well as thioflavin-T fluorescence assays and
                      transmission electron microscopy. We found that the
                      aggregation was inhibited significantly when the
                      concentration of calcium-free Ator exceeded that of Aβ by
                      at least a factor of 2. The 1H–15N heteronuclear single
                      quantum correlation and saturation-transfer difference NMR
                      data suggest that calcium-free Ator exerts its effect
                      through interaction with the 16KLVF19 binding site on the
                      Aβ peptide via its aromatic rings as well as hydroxyl and
                      methyl groups. On the other hand, molecular dynamics
                      simulations confirmed that the increasing concentration of
                      Ator is necessary for the inhibition of the conformational
                      transition of Aβ from an α-helix-dominant to a
                      β-sheet-dominant structure.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35104501},
      UT           = {WOS:000794865600002},
      doi          = {10.1016/j.jbc.2022.101662},
      url          = {https://juser.fz-juelich.de/record/996128},
}