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@ARTICLE{Rsener:851774,
      author       = {Rösener, Nadine and Gremer, Lothar and Reinartz, Elke and
                      König, Anna and Brener, Oleksandr and Heise, Henrike and
                      Hoyer, Wolfgang and Neudecker, Philipp and Willbold, Dieter},
      title        = {{A} {D}-enantiomeric peptide interferes with
                      hetero-association of amyloid-β oligomers and prion
                      protein},
      journal      = {The journal of biological chemistry},
      volume       = {293},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2018-05289},
      pages        = {jbc.RA118.003116 -},
      year         = {2018},
      abstract     = {Alzheimer’s disease (AD) is a progressive
                      neurodegenerative disorder that affects millions of people
                      worldwide. One AD hallmark is the aggregation of amyloid-β
                      (Aβ) into soluble oligomers and insoluble fibrils. Several
                      studies have reported that oligomers rather than fibrils are
                      the most toxic species in AD progression. Aβ oligomers bind
                      with high affinity to membrane-associated prion protein
                      (PrP), leading to toxic signaling across the cell membrane,
                      which makes the Aβ–PrP interaction an attractive
                      therapeutic target. Here, probing this interaction in more
                      detail, we found that both full-length, soluble human (hu)
                      PrP(23–230) and huPrP(23–144), lacking the globular
                      C-terminal domain, bind to Aβ oligomers to form large
                      complexes above the megadalton size range. Following
                      purification by sucrose density–gradient
                      ultracentrifugation, the Aβ and huPrP contents in these
                      hetero-assemblies were quantified by reversed-phase HPLC.
                      The Aβ:PrP molar ratio in these assemblies exhibited some
                      limited variation depending on the molar ratio of the
                      initial mixture. Specifically, a molar ratio of about four
                      Aβ to one huPrP in the presence of an excess of
                      huPrP(23–230) or huPrP(23–144) suggested that four Aβ
                      units are required to form one huPrP-binding site. Of note,
                      an Aβ-binding all-D-enantiomeric peptide, RD2D3, competed
                      with huPrP for Aβ oligomers and interfered with Aβ–PrP
                      hetero-assembly in a concentration-dependent manner. Our
                      results highlight the importance of multivalent epitopes on
                      Aβ oligomers for Aβ–PrP interactions and have yielded an
                      all-D-peptide-based, therapeutically promising agent that
                      competes with PrP for these interactions.},
      cin          = {ICS-6},
      ddc          = {570},
      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:30131337},
      UT           = {WOS:000447256000001},
      doi          = {10.1074/jbc.RA118.003116},
      url          = {https://juser.fz-juelich.de/record/851774},
}