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@ARTICLE{Han:1048115,
      author       = {Han, Mookyoung and Frieg, Benedikt and Matthes, Dirk and
                      Leonov, Andrei and Ryazanov, Sergey and Giller, Karin and
                      Nimerovsky, Evgeny and Stampolaki, Marianna and Xue, Kai and
                      Overkamp, Kerstin and Dienemann, Christian and Riedel,
                      Dietmar and Giese, Armin and Becker, Stefan and de Groot,
                      Bert L. and Schröder, Gunnar F. and Andreas, Loren B. and
                      Griesinger, Christian},
      title        = {{A}nle138b binds predominantly to the central cavity in
                      lipidic {A}β₄₀ fibrils and modulates fibril formation},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2025-04506},
      pages        = {8850},
      year         = {2025},
      abstract     = {Alzheimer’s disease is a specific neurodegenerative
                      disorder, distinct from normal aging, with a growing unmet
                      medical need. It is characterized by the accumulation of
                      amyloid plaques in the brain, primarily consisting of
                      amyloid beta (Aβ) fibrils. Therapeutic antibodies can slow
                      down the disease, but are associated with potential severe
                      side effects, motivating the development of small molecules
                      to halt disease progression. This study investigates the
                      interaction between the clinical drug candidate small
                      molecule anle138b and lipidic Aβ₄₀ fibrils of type 1
                      (L1). L1 fibrils were previously shown to closely resemble
                      fibrils from Alzheimer’s patients. Using high-resolution
                      structural biology techniques, including cryo-electron
                      microscopy (cryo-EM), nuclear magnetic resonance (NMR)
                      spectroscopy enhanced by dynamic nuclear polarization (DNP),
                      and molecular dynamics (MD) simulations, we find that
                      anle138b selectively binds to a cavity within the fibril.
                      This structural insight provides a deeper understanding of a
                      potential drug-binding mechanism at the atomic level andmay
                      inform the development of therapies and diagnostic
                      approaches. In addition, anle138b reduces fibril formation
                      in the presence of lipids by approximately $75\%.$ Thismay
                      suggest amechanistic connection to its previously reported
                      activity in animal models of Alzheimer’s disease.},
      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},
      doi          = {10.1038/s41467-025-64443-6},
      url          = {https://juser.fz-juelich.de/record/1048115},
}