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@ARTICLE{Klein:809114,
      author       = {Klein, Antonia Nicole and Ziehm, Tamar and Tusche, Markus
                      and Buitenhuis, Johan and Bartnik, Dirk and Boeddrich,
                      Annett and Wiglenda, Thomas and Wanker, Erich and Funke,
                      Susanne Aileen and Brener, Oleksandr and Gremer, Lothar and
                      Kutzsche, Janine and Willbold, Dieter},
      title        = {{O}ptimization of the {A}ll-{D} {P}eptide {D}3 for {A}β
                      {O}ligomer {E}limination},
      journal      = {PLoS one},
      volume       = {11},
      number       = {4},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-02505},
      pages        = {e0153035 -},
      year         = {2016},
      abstract     = {The aggregation of amyloid-β (Aβ) is postulated to be the
                      crucial event in Alzheimer’s disease (AD). In particular,
                      small neurotoxic Aβ oligomers are considered to be
                      responsible for the development and progression of AD.
                      Therefore, elimination of thesis oligomers represents a
                      potential causal therapy of AD. Starting from the
                      well-characterized D-enantiomeric peptide D3, we identified
                      D3 derivatives that bind monomeric Aβ. The underlying
                      hypothesis is that ligands bind monomeric Aβ and stabilize
                      these species within the various equilibria with Aβ
                      assemblies, leading ultimately to the elimination of Aβ
                      oligomers. One of the hereby identified D-peptides, DB3, and
                      a head-to-tail tandem of DB3, DB3DB3, were studied in
                      detail. Both peptides were found to: (i) inhibit the
                      formation of Thioflavin T-positive fibrils; (ii) bind to Aβ
                      monomers with micromolar affinities; (iii) eliminate Aβ
                      oligomers; (iv) reduce Aβ-induced cytotoxicity; and (v)
                      disassemble preformed Aβ aggregates. The beneficial effects
                      of DB3 were improved by DB3DB3, which showed highly enhanced
                      efficacy. Our approach yielded Aβ monomer-stabilizing
                      ligands that can be investigated as a suitable therapeutic
                      strategy against AD.},
      cin          = {ICS-6 / ICS-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ICS-3-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553) / 551 -
                      Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-553 / G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000374565100009},
      doi          = {10.1371/journal.pone.0153035},
      url          = {https://juser.fz-juelich.de/record/809114},
}