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@ARTICLE{Zhang:872743,
      author       = {Zhang, Tao and Gering, Ian and Kutzsche, Janine and
                      Nagel-Steger, Luitgard and Willbold, Dieter},
      title        = {{T}oward the {M}ode of {A}ction of the {C}linical {S}tage
                      {A}ll- d -{E}nantiomeric {P}eptide {RD}2 on {A}β42
                      {A}ggregation},
      journal      = {ACS chemical neuroscience},
      volume       = {10},
      number       = {12},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2020-00221},
      pages        = {4800 - 4809},
      year         = {2019},
      abstract     = {The aggregation of amyloid-β (Aβ) into oligomers and
                      fibrillary structures is critical for the pathogenesis of
                      Alzheimer’s disease (AD). Recently, research effort has
                      been focused on developing novel agents that can
                      preferentially suppress Aβ oligomer mediated toxicities,
                      for example, by directly targeting these toxic assemblies.
                      The compound RD2 has been developed and optimized for Aβ42
                      monomer binding and stabilization of the monomer in its
                      native intrinsically disordered conformation. It has been
                      demonstrated to improve and even reverse the cognitive and
                      behavioral deficits in AD mouse models, while the detailed
                      mechanism of action is not fully clarified. Here we focused
                      on exploring the interaction between RD2 and Aβ42 monomers
                      and its consequences for the fibrillation of Aβ42. RD2
                      binds to Aβ42 monomers with nanomolar affinities, according
                      to microscale thermophoresis and surface plasmon resonance
                      measurements. Complexes between RD2 and Aβ42 monomers are
                      formed at 1:1 and other stoichiometries, as revealed by
                      analytical ultracentrifugation. At substoichiometric levels,
                      RD2 slows down the secondary structure conversion of Aβ42
                      and significantly delays the fibril formation. Our research
                      provides experimental evidence in supporting that RD2
                      eliminates toxic Aβ assemblies by stabilizing Aβ monomers
                      in their native intrinsically disordered conformation. The
                      study further supports the promising application of RD2 in
                      counteracting Aβ aggregation related pathologies.},
      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:31710458},
      UT           = {WOS:000503918400005},
      doi          = {10.1021/acschemneuro.9b00458},
      url          = {https://juser.fz-juelich.de/record/872743},
}