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@ARTICLE{Fatafta:873655,
      author       = {Fatafta, Hebah and Poojari, Chetan and Sayyed-Ahmad,
                      Abdallah and Strodel, Birgit and Owen, Michael},
      title        = {{R}ole of {O}xidized {G}ly25, {G}ly29, and {G}ly33
                      {R}esidues on the {I}nteractions of {A}β 1–42 with
                      {L}ipid {M}embranes},
      journal      = {ACS chemical neuroscience},
      volume       = {11},
      number       = {4},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2020-00886},
      pages        = {535-548},
      year         = {2020},
      abstract     = {Oxidative stress is known to play an important role in the
                      pathogenesis of Alzheimer's disease. Moreover, it is
                      becoming increasingly evident that the plasma membrane of
                      neurons plays a role in modulating the aggregation and
                      toxicity of Alzheimer's amyloid-β peptide (Aβ). In this
                      study, the combined and interdependent effects of oxidation
                      and membrane interactions on the 42 residues long Aβ
                      isoform are investigated using molecular simulations.
                      Hamiltonian replica exchange molecular dynamics simulations
                      are utilized to elucidate the impact of selected oxidized
                      glycine residues of Aβ42 on the interactions of the peptide
                      with a model membrane comprised of $70\%$ POPC, $25\%$
                      cholesterol, and $5\%$ of the ganglioside GM1. The main
                      findings are that, independent of the oxidation state, Aβ
                      prefers binding to GM1 over POPC, which is further enhanced
                      by the oxidation of Gly29 and Gly33 and reduced the
                      formation of β-sheet. Our results suggest that the
                      differences observed in Aβ42 conformations and its
                      interaction with a lipid bilayer upon oxidation originate
                      from the position of the oxidized Gly residue with respect
                      to the hydrophobic sequence of Aβ42 involving the
                      Gly29-XXX-Gly33-XXX-Gly37 motif and from specific
                      interactions between the peptide and the terminal sugar
                      groups of GM1.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31939658},
      UT           = {WOS:000515195800005},
      doi          = {10.1021/acschemneuro.9b00558},
      url          = {https://juser.fz-juelich.de/record/873655},
}