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@ARTICLE{Dammers:826171,
      author       = {Dammers, Christina and Yolcu, Deniz and Kukuk, Laura and
                      Willbold, Dieter and Pickhardt, Marcus and Mandelkow,
                      Eckhard and Horn, Anselm H. C. and Sticht, Heinrich and
                      Malhis, Marwa Nidal and Will, Nadja and Schuster, Judith and
                      Funke, Aileen},
      title        = {{S}election and {C}haracterization of {T}au {B}inding
                      {D}-{E}nantiomeric {P}eptides with {P}otential for {T}herapy
                      of {A}lzheimer {D}isease},
      journal      = {PLoS one},
      volume       = {11},
      number       = {12},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2017-00417},
      pages        = {e0167432},
      year         = {2016},
      abstract     = {A variety of neurodegenerative disorders, including
                      Alzheimer disease (AD), are associated with neurofibrillary
                      tangles composed of the tau protein, as well as toxic tau
                      oligomers. Inhibitors of pathological tau aggregation,
                      interrupting tau self-assembly, might be useful for the
                      development of therapeutics. Employing mirror image phage
                      display with a large peptide library (over 109 different
                      peptides), we have identified tau fibril binding peptides
                      consisting of d-enantiomeric amino acids. d-enantiomeric
                      peptides are extremely protease stable and not or less
                      immunogenic than l-peptides, and the suitability of
                      d-peptides for in vivo applications have already been
                      demonstrated. Phage display selections were performed using
                      fibrils of the d-enantiomeric hexapeptide VQIVYK,
                      representing residues 306 to 311 of the tau protein, as a
                      target. VQIVYK has been demonstrated to be important for
                      fibril formation of the full lengths protein and forms
                      fibrils by itself. Here, we report on d-enantiomeric
                      peptides, which bind to VQIVYK, tau isoforms like tau3RD
                      (K19) as well as to full lengths tau fibrils, and modulate
                      the aggregation of the respective tau form. The peptides are
                      able to penetrate cells and might be interesting for
                      therapeutic and diagnostic applications in AD research.},
      cin          = {ICS-6},
      ddc          = {500},
      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},
      UT           = {WOS:000392843200017},
      pubmed       = {pmid:28006031},
      doi          = {10.1371/journal.pone.0167432},
      url          = {https://juser.fz-juelich.de/record/826171},
}