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@ARTICLE{Sevenich:917327,
      author       = {Sevenich, Marc and Honold, Dominik and Willuweit, Antje and
                      Kutzsche, Janine and Mohrlüder, Jeannine and Willbold,
                      Dieter},
      title        = {{D}evelopment of an α-synuclein fibril and oligomer
                      specific tracer for diagnosis of {P}arkinson's disease,
                      dementia with {L}ewy bodies and multiple system atrophy},
      journal      = {Neurochemistry international},
      volume       = {161},
      issn         = {0197-0186},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2023-00555},
      pages        = {105422 -},
      year         = {2022},
      abstract     = {The development of specific disease-associated PET tracers
                      is one of the major challenges, the realization of which in
                      neurodegenerative diseases would enable not only the
                      efficiency of diagnosis but also support the development of
                      disease-modifying therapeutics. Parkinson's disease (PD) is
                      the most common neurodegenerative movement disorder and is
                      characterized by neuronal fibrillary inclusions composed of
                      aggregated α-synuclein (α-syn). However, these deposits
                      are not only found in PD, but also in other related diseases
                      such as multiple system atrophy (MSA) and dementia with Lewy
                      bodies (DLB), which are grouped under the term
                      synucleinopathies. In this study, we used NGS-guided phage
                      display selection to identify short peptides that bind
                      aggregated α-syn. By surface plasmon resonance (SPR)-based
                      affinity screening, we identified the peptide SVLfib-5 that
                      recognizes aggregated α-syn with high complex stability and
                      sequence specificity. Further analysis SPR showed that
                      SVLfib-5 is not only specific for aggregated α-syn, but in
                      particular recognizes fibrillary and oligomeric structures.
                      Moreover, fluorescence microscopy of human brain tissue
                      sections from PD, MSA, and DLB patients with SVLfib-5
                      allowed specific recognition of α-syn and a clear
                      discrimination between diseased and non-diseased samples.
                      These findings provide the basis for the further development
                      of an α-syn PET tracer for early diagnosis and monitoring
                      of disease progression and therapy progress.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / SFB 1208 B02 - Identität und Dynamik von
                      Membransystemen - von Molekülen bis zu zellulären
                      Funktionen (267205415)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(GEPRIS)267205415},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36252819},
      UT           = {WOS:000880099200004},
      doi          = {10.1016/j.neuint.2022.105422},
      url          = {https://juser.fz-juelich.de/record/917327},
}