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@ARTICLE{Fatafta:902423,
      author       = {Fatafta, Hebah and Khaled, Mohammed and Owen, Michael C.
                      and Sayyed-Ahmad, Abdallah and Strodel, Birgit},
      title        = {{A}myloid-β peptide dimers undergo a random coil to
                      β-sheet transition in the aqueous phase but not at the
                      neuronal membrane},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {118},
      number       = {39},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2021-04245},
      pages        = {e2106210118 -},
      year         = {2021},
      abstract     = {Mounting evidence suggests that the neuronal cell membrane
                      is the main site of oligomer-mediated neuronal toxicity of
                      amyloid-β peptides in Alzheimer’s disease. To gain a
                      detailed understanding of the mutual interference of
                      amyloid-β oligomers and the neuronal membrane, we carried
                      out microseconds of all-atom molecular dynamics (MD)
                      simulations on the dimerization of amyloid-β (Aβ)42 in the
                      aqueous phase and in the presence of a lipid bilayer
                      mimicking the in vivo composition of neuronal membranes. The
                      dimerization in solution is characterized by a random coil
                      to β-sheet transition that seems on pathway to amyloid
                      aggregation, while the interactions with the neuronal
                      membrane decrease the order of the Aβ42 dimer by
                      attenuating its propensity to form a β-sheet structure. The
                      main lipid interaction partners of Aβ42 are the
                      surface-exposed sugar groups of the gangliosides GM1. As the
                      neurotoxic activity of amyloid oligomers increases with
                      oligomer order, these results suggest that GM1 is
                      neuroprotective against Aβ-mediated toxicity.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {552 - Engineering Cell Function (POF3-552) / 5244 -
                      Information Processing in Neuronal Networks (POF4-524)},
      pid          = {G:(DE-HGF)POF3-552 / G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34544868},
      UT           = {WOS:000708052600007},
      doi          = {10.1073/pnas.2106210118},
      url          = {https://juser.fz-juelich.de/record/902423},
}