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@ARTICLE{Wiesehan:338,
      author       = {Wiesehan, K. and Stöhr, J. and Nagel-Steger, K. and van
                      Groen, T. and Riesner, D. and Willbold, D.},
      title        = {{I}nhibition of cytotoxicity and amyloid fibril formation
                      by a {D}-amino acid peptide that specifically binds to
                      {A}lzheimer's disease amyloid peptide},
      journal      = {Protein engineering design and selection},
      volume       = {21},
      issn         = {1741-0126},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PreJuSER-338},
      pages        = {241 - 246},
      year         = {2008},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Alzheimer's disease (AD) is a progressive neurodegenerative
                      disorder. The 'amyloid cascade hypothesis' assigns the
                      amyloid-beta-peptide (Abeta) a central role in the
                      pathogenesis of AD. Although it is not yet established,
                      whether the resulting Abeta aggregates are the causative
                      agent or just a result of the disease progression,
                      polymerization of Abeta has been identified as a major
                      feature during AD pathogenesis. Inhibition of the Abeta
                      polymer formation, thus, has emerged as a potential
                      therapeutic approach. In this context, we identified
                      peptides consisting of d-enantiomeric amino acid peptides
                      (d-peptides) that bind to Abeta. D-peptides are known to be
                      more protease resistant and less immunogenic than the
                      respective L-enantiomers. Previously, we have shown that a
                      12mer D-peptide specifically binds to Abeta amyloid plaques
                      in brain tissue sections from former AD patients. In vitro
                      obtained binding affinities to synthetic Abeta revealed a
                      K(d) value in the submicromolar range. The aim of the
                      present study was to investigate the influence of this
                      d-peptide to Abeta polymerization and toxicity. Using cell
                      toxicity assays, thioflavin fluorescence, fluorescence
                      correlation spectroscopy and electron microscopy, we found a
                      significant effect of the d-peptide on both. Presence of
                      D-peptides (dpep) reduces the average size of Abeta
                      aggregates, but increases their number. In addition, Abeta
                      cytotoxicity on PC12 cells is reduced in the presence of
                      dpep.},
      keywords     = {Amyloid beta-Peptides: antagonists $\&$ inhibitors /
                      Amyloid beta-Peptides: metabolism / Amyloid beta-Peptides:
                      toxicity / Animals / Cell Death: drug effects / Cytotoxins:
                      antagonists $\&$ inhibitors / Cytotoxins: metabolism /
                      Cytotoxins: toxicity / Microscopy, Electron / PC12 Cells /
                      Peptides: chemistry / Peptides: metabolism / Peptides:
                      pharmacology / Polymers: metabolism / Protein Binding /
                      Protein Structure, Secondary: drug effects / Rats /
                      Spectrometry, Fluorescence / Substrate Specificity /
                      Thiazoles: metabolism / Amyloid beta-Peptides (NLM
                      Chemicals) / Cytotoxins (NLM Chemicals) / Peptides (NLM
                      Chemicals) / Polymers (NLM Chemicals) / Thiazoles (NLM
                      Chemicals) / thioflavin T (NLM Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biotechnology $\&$
                      Applied Microbiology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18252750},
      UT           = {WOS:000254295200003},
      doi          = {10.1093/protein/gzm054},
      url          = {https://juser.fz-juelich.de/record/338},
}