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@ARTICLE{Antonschmidt:912259,
      author       = {Antonschmidt, Leif and Matthes, Dirk and Dervişoğlu,
                      Rıza and Frieg, Benedikt and Dienemann, Christian and
                      Leonov, Andrei and Nimerovsky, Evgeny and Sant, Vrinda and
                      Ryazanov, Sergey and Giese, Armin and Schröder, Gunnar F.
                      and Becker, Stefan and de Groot, Bert L. and Griesinger,
                      Christian and Andreas, Loren B.},
      title        = {{T}he clinical drug candidate anle138b binds in a cavity of
                      lipidic α-synuclein fibrils},
      journal      = {Nature Communications},
      volume       = {13},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2022-05456},
      pages        = {5385},
      year         = {2022},
      abstract     = {Aggregation of amyloidogenic proteins is a characteristic
                      of multiple neurodegenerative diseases. Atomic resolution of
                      small molecule binding to such pathological protein
                      aggregates is of interest for the development of
                      therapeutics and diagnostics. Here we investigate the
                      interaction between α-synuclein fibrils and anle138b, a
                      clinical drug candidate for disease modifying therapy in
                      neurodegeneration and a promising scaffold for positron
                      emission tomography tracer design. We used nuclear magnetic
                      resonance spectroscopy and the cryogenic electron microscopy
                      structure of α-synuclein fibrils grown in the presence of
                      lipids to locate anle138b within a cavity formed between two
                      β-strands. We explored and quantified multiple binding
                      modes of the compound in detail using molecular dynamics
                      simulations. Our results reveal stable polar interactions
                      between anle138b and backbone moieties inside the tubular
                      cavity of the fibrils. Such cavities are common in other
                      fibril structures as well.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36104315},
      UT           = {WOS:000853935100020},
      doi          = {10.1038/s41467-022-32797-w},
      url          = {https://juser.fz-juelich.de/record/912259},
}