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@ARTICLE{Zhang:863067,
      author       = {Zhang, Tao and Loschwitz, Jennifer and Strodel, Birgit and
                      Nagel-Steger, Luitgard and Willbold, Dieter},
      title        = {{I}nterference with {A}myloid-β {N}ucleation by
                      {T}ransient {L}igand {I}nteraction},
      journal      = {Molecules},
      volume       = {24},
      number       = {11},
      issn         = {1420-3049},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2019-03184},
      pages        = {2129 -},
      year         = {2019},
      abstract     = {Amyloid-β peptide (Aβ) is an intrinsically disordered
                      protein (IDP) associated with Alzheimer’s disease. The
                      structural flexibility and aggregation propensity of Aβ
                      pose major challenges for elucidating the interaction
                      between Aβ monomers and ligands. All-D-peptides consisting
                      solely of D-enantiomeric amino acid residues are interesting
                      drug candidates that combine high binding specificity with
                      high metabolic stability. Here we characterized the
                      interaction between the 12-residue all-D-peptide D3 and
                      Aβ42 monomers, and how the interaction influences Aβ42
                      aggregation. We demonstrate for the first time that D3 binds
                      to Aβ42 monomers with submicromolar affinities. These two
                      highly unstructured molecules are able to form complexes
                      with 1:1 and other stoichiometries. Further, D3 at
                      substoichiometric concentrations effectively slows down the
                      β-sheet formation and Aβ42 fibrillation by modulating the
                      nucleation process. The study provides new insights into the
                      molecular mechanism of how D3 affects Aβ assemblies and
                      contributes to our knowledge on the interaction between two
                      IDPs.},
      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:31195746},
      UT           = {WOS:000472631000102},
      doi          = {10.3390/molecules24112129},
      url          = {https://juser.fz-juelich.de/record/863067},
}