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@ARTICLE{Deike:889722,
      author       = {Deike, Stefanie and Rothemund, Sven and Voigt, Bruno and
                      Samantray, Suman and Strodel, Birgit and Binder, Wolfgang
                      H.},
      title        = {β-{T}urn mimetic synthetic peptides as amyloid-β
                      aggregation inhibitors},
      journal      = {Bioorganic chemistry},
      volume       = {101},
      issn         = {0045-2068},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {FZJ-2021-00344},
      pages        = {104012 -},
      year         = {2020},
      abstract     = {Aggregation of amyloid peptides results in severe
                      neurodegenerative diseases. While the fibril structures of
                      Aβ40and Aβ42 have been described recently, resolution of
                      the aggregation pathway and evaluation of potent
                      inhibitorsstill remains elusive, in particular in view of
                      the hairpin-region of Aβ40. We here report the
                      preparationof beta-turn mimetic conjugates containing
                      synthetic turn mimetic structures in the turn region of
                      Aβ40 and Aβ16-35, replacing 2 amino acids in the
                      turn-region G25 – K28. The structure of the turn mimic
                      induces both, accelerationof fibrillation and the complete
                      inhibition of fibrillation, confirming the importance of the
                      turn regionon the aggregation. Replacing position G25-S26
                      provided the best inhibition effect for both beta-turn
                      mimetics,the bicyclic BTD 1 and the aromatic TAA 2, while
                      positions N27-K28 and V24-G25 showed only weaker or
                      noinhibitory effects. When comparing different turn mimetics
                      at the same position (G25-S26), conjugate 1a bearingthe BTD
                      turn showed the best inhibition of Aβ40 aggregation, while
                      5-amino-valeric acid 4a showed the weakesteffect. Thus there
                      is a pronounced impact on fibrillation with the chemical
                      nature of the embedded beta-turnmimic:the conformationally
                      constrained turns 1 and 2 lead to a significantly reduced
                      fibrillation, even inhibitingfibrillation of native Aβ40
                      when added in amounts down to 1/10, whereas the more
                      flexible beta-turn-mimics 4-amino-benzoic acid 3a and
                      5-amino-valeric acid 4a lead to enhanced fibrillation.
                      Toxicity-testing of the mostsuccessful conjugate showed only
                      minor toxicity in cell-viability assays using the N2a cell
                      line. Structuraldownsizing lead to the short fragment
                      BTD/peptide Aβ16-35 as inhibitor of the aggregation of
                      Aβ40, opening largepotential for further small peptide
                      based inhibitors.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32683138},
      UT           = {WOS:000552635800006},
      doi          = {10.1016/j.bioorg.2020.104012},
      url          = {https://juser.fz-juelich.de/record/889722},
}