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@ARTICLE{Cavini:856101,
      author       = {Cavini, Italo A. and Munte, Claudia E. and Erlach, Markus
                      Beck and van Groen, Thomas and Kadish, Inga and Zhang, Tao
                      and Ziehm, Tamar and Nagel-Steger, Luitgard and Kutzsche,
                      Janine and Kremer, Werner and Willbold, Dieter and
                      Kalbitzer, Hans Robert},
      title        = {{I}nhibition of amyloid {A}β aggregation by high pressures
                      or specific {D}-enantiomeric peptides},
      journal      = {Chemical communications},
      volume       = {54},
      number       = {26},
      issn         = {1364-548X},
      address      = {Cambridge},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-05747},
      pages        = {3294 - 3297},
      year         = {2018},
      abstract     = {Pressure can shift the polymer–monomer equilibrium of
                      Aβ, increasing pressure first leads to a release of
                      Aβ-monomers, surprisingly at pressures higher than 180 MPa
                      repolymerization is induced. By high pressure NMR
                      spectroscopy, differences of partial molar volumes ΔV0 and
                      compressibility factors Δβ′ of polymerization were
                      determined at different temperatures. The D-enantiomeric
                      peptides RD2 and RD2D3 bind to monomeric Aβ with affinities
                      substantially higher than those determined for fibril
                      formation. By reducing the Aβ concentration below the
                      critical concentration for polymerization they inhibit the
                      formation of toxic oligomers. Chemical shift perturbation
                      allows the identification of the binding sites. The
                      D-peptides are candidates for drugs preventing Alzheimer's
                      disease. We show that RD2D3 has a positive effect on the
                      cognitive behaviour of transgenic (APPSwDI) mice prone to
                      Alzheimer's disease. The heterodimer complexes have a
                      smaller Stokes radius than Aβ alone indicating the
                      recognition of a more compact conformation of Aβ identified
                      by high pressure NMR before.},
      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:29537428},
      UT           = {WOS:000428553500024},
      doi          = {10.1039/C8CC01458B},
      url          = {https://juser.fz-juelich.de/record/856101},
}