Home > Publications database > Evaluation of the 18F-Labeled Analog of the Therapeutic All-d-enantiomeric Peptide RD2 for Amyloid β Imaging > print

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005     20240408211951.0
024 7 _ |a 10.1016/j.ejps.2023.106421
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024 7 _ |a 0928-0987
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024 7 _ |a 1879-0720
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100 1 _ |a Willuweit, Antje
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245 _ _ |a Evaluation of the 18F-Labeled Analog of the Therapeutic All-d-enantiomeric Peptide RD2 for Amyloid β Imaging
260 _ _ |a New York, NY [u.a.]
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520 _ _ |a 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.
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700 1 _ |a Schöneck, Michael
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