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@ARTICLE{vanGroen:3797,
      author       = {van Groen, T. and Kadish, I. and Wiesehan, K. and Funke, S.
                      A. and Willbold, D.},
      title        = {{I}n vitro and in vivo staining characteristics of small,
                      fluorescent, {A}ß42 binding {D}-enantiomeric peptides in
                      transgenic {AD} mouse models},
      journal      = {ChemMedChem},
      volume       = {4},
      issn         = {1860-7179},
      address      = {Weinheim [u.a.]},
      publisher    = {Wiley-VCH},
      reportid     = {PreJuSER-3797},
      pages        = {276 - 282},
      year         = {2009},
      note         = {This work was supported by a grant from the
                      Volkswagen-Stiftung to D.W. (1/82 649).},
      abstract     = {One of the characteristic pathological hallmarks of
                      Alzheimer's disease (AD) are neuritic plaques that consist
                      of amyloid peptide (Abeta). To improve diagnosis and
                      treatment evaluation, neuroimaging tools that make use of
                      Abeta-binding ligands to visualise amyloid plaques are being
                      developed. We investigate the in vitro and in vivo
                      characteristics of a series of three D-enantiomeric peptides
                      (D1-D3) that were developed to specifically bind amyloid
                      beta1-42 (Abeta42) in the brains of transgenic AD-model
                      mice. We stained brain sections of the mice, injected and
                      infused the mice with these small D-peptides, and examined
                      their staining of Abeta42 in the brain. The experiments
                      demonstrate that the D-peptides label all plaques that
                      contain Abeta42 in the brain. In contrast, diffuse amyloid
                      beta deposits (which do not contain Abeta42) are not stained
                      by any of the D-peptides. The in vivo and in vitro studies
                      demonstrate that the D-peptides label all Abeta42 in the
                      brain, and none of the D-peptides causes inflammation or is
                      taken up by astrocytes or microglia. Furthermore, long-term
                      infusion of the peptides does not cause inflammation.
                      Together, this demonstrates that these D-peptides might be
                      suitable for use as molecular probes to measure Abeta plaque
                      load in the living brain for early diagnosis of Alzheimer's
                      disease, or to monitor Abeta42 plaque load during disease
                      progression or during treatment.},
      keywords     = {Alzheimer Disease: metabolism / Amino Acid Sequence /
                      Amyloid beta-Peptides: chemistry / Amyloid beta-Peptides:
                      metabolism / Animals / Disease Models, Animal / Fluorescent
                      Dyes: chemistry / Mice / Mice, Transgenic / Peptide
                      Fragments: chemistry / Peptide Fragments: metabolism /
                      Peptides: metabolism / Protein Binding / Stereoisomerism /
                      Amyloid beta-Peptides (NLM Chemicals) / Fluorescent Dyes
                      (NLM Chemicals) / Peptide Fragments (NLM Chemicals) /
                      Peptides (NLM Chemicals) / amyloid beta-protein (1-42) (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Chemistry, Medicinal / Pharmacology $\&$ Pharmacy},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19072935},
      UT           = {WOS:000263803200016},
      doi          = {10.1002/cmdc.200800289},
      url          = {https://juser.fz-juelich.de/record/3797},
}