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@ARTICLE{Willuweit:1005300,
      author       = {Willuweit, Antje and Humpert, Swen and Schöneck, Michael
                      and Endepols, Heike and Burda, Nicole and Gremer, Lothar and
                      Gering, Ian and Kutzsche, Janine and Shah, N. Jon and
                      Langen, Karl-Josef and Neumaier, Bernd and Willbold, Dieter
                      and Drzezga, Alexander},
      title        = {{E}valuation of the 18{F}-{L}abeled {A}nalog of the
                      {T}herapeutic {A}ll-d-enantiomeric {P}eptide {RD}2 for
                      {A}myloid β {I}maging},
      journal      = {European journal of pharmaceutical sciences},
      volume       = {184},
      issn         = {0928-0987},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-01412},
      pages        = {106421},
      year         = {2023},
      abstract     = {Positron emission tomography (PET) imaging with
                      radiotracers that bind to fibrillary amyloid β (Aβ)
                      deposits is an important tool for the diagnosis of
                      Alzheimer's disease (AD) and for the recruitment of patients
                      into clinical trials. However, it has been suggested that
                      rather than the fibrillary Aβ deposits, it is smaller,
                      soluble Aβ aggregates that exert a neurotoxic effect and
                      trigger AD pathogenesis. The aim of the current study is to
                      develop a PET probe that is capable of detecting small
                      aggregates and soluble Aβ oligomers for improved diagnosis
                      and therapy monitoring. An 18F-labeled radioligand was
                      prepared based on the Aβ-binding d-enantiomeric peptide
                      RD2, which is currently being evaluated in clinical trials
                      as a therapeutic agent to dissolve Aβ oligomers.
                      18F-labeling was carried out using palladium-catalyzed
                      S-arylation of RD2 with 2-[18F]fluoro-5-iodopyridine
                      ([18F]FIPy). Specific binding of [18F]RD2-cFPy to brain
                      material from transgenic AD (APP/PS1) mice and AD patients
                      was demonstrated with in vitro autoradiography. In vivo
                      uptake and biodistribution of [18F]RD2-cFPy were evaluated
                      using PET analyses in wild-type and transgenic APP/PS1 mice.
                      Although brain penetration and brain wash-out kinetics of
                      the radioligand were low, this study provides proof of
                      principle for a PET probe based on a d-enantiomeric peptide
                      binding to soluble Aβ species.},
      cin          = {INM-4 / INM-5 / IBI-7 / INM-2 / INM-11 / JARA-BRAIN},
      ddc          = {610},
      cid          = {I:(DE-Juel1)INM-4-20090406 / I:(DE-Juel1)INM-5-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)INM-2-20090406 /
                      I:(DE-Juel1)INM-11-20170113 / $I:(DE-82)080010_20140620$},
      pnm          = {5253 - Neuroimaging (POF4-525) / 5244 - Information
                      Processing in Neuronal Networks (POF4-524) / 5252 - Brain
                      Dysfunction and Plasticity (POF4-525)},
      pid          = {G:(DE-HGF)POF4-5253 / G:(DE-HGF)POF4-5244 /
                      G:(DE-HGF)POF4-5252},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36889654},
      UT           = {WOS:000956437600001},
      doi          = {10.1016/j.ejps.2023.106421},
      url          = {https://juser.fz-juelich.de/record/1005300},
}