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@ARTICLE{Sevenich:1046551,
      author       = {Sevenich, Marc and Gering, Ian and Kass, Bettina and
                      Vollmer, Madita and Aghabashlou Saisan, Selma and Tusche,
                      Markus and Kupreichyk, Tatsiana and Pauly, Thomas and
                      Stoldt, Matthias and Hoyer, Wolfgang and Willuweit, Antje
                      and Kutzsche, Janine and Lakomek, Nils-Alexander and
                      Nagel-Steger, Luitgard and Gremer, Lothar and Tamgüney,
                      Gültekin and Mohrlüder, Jeannine and Willbold, Dieter},
      title        = {{D}irect disassembly of α-syn preformed fibrils into
                      α-syn monomers by an all-{D}-peptide},
      journal      = {npj Parkinson's Disease},
      volume       = {11},
      number       = {1},
      issn         = {2373-8057},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2025-03861},
      pages        = {271},
      year         = {2025},
      abstract     = {A hallmark of Parkinson's disease (PD) is the progressive
                      neurodegeneration associated with soluble oligomeric and
                      fibrillar forms of misfolded α-synuclein (α-syn). In this
                      study, all-D-enantiomeric peptide ligands are presented that
                      bind monomeric α-syn with high affinity, stabilize its
                      physiological monomeric status, prevent aggregation and
                      dissolve existing aggregates. This "antiprionic" mode of
                      action directly targets pathogenic aggregated particles.
                      Using mirror-image phage display on D-enantiomeric
                      full-length α-syn, SVD-1 and SVD-1a were identified,
                      showing a delay of aggregation and reduction of aggregate
                      formation in both de novo and seeded models. Picomolar KDs
                      were confirmed by SPR, where a highly dynamic interaction
                      mode was verified by PRE-NMR. SVD-1a also reduced the
                      toxicity and intracellular seeding of α-syn fibrils in cell
                      culture by disassembling them into monomers, as confirmed by
                      atomic force microscopy and dynamic light scattering. These
                      results support SVD-1a as a promising lead compound for the
                      treatment of Parkinson's disease.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40983605},
      UT           = {WOS:001575814700001},
      doi          = {10.1038/s41531-025-01132-7},
      url          = {https://juser.fz-juelich.de/record/1046551},
}