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@ARTICLE{sterlund:858908,
      author       = {Österlund, Nicklas and Kulkarni, Yashraj S. and Misiaszek,
                      Agata D. and Wallin, Cecilia and Krüger, Dennis M. and
                      Liao, Qinghua and Mashayekhy Rad, Farshid and Jarvet, Jüri
                      and Strodel, Birgit and Wärmländer, Sebastian K. T. S. and
                      Ilag, Leopold L. and Kamerlin, Shina C. L. and Gräslund,
                      Astrid},
      title        = {{A}myloid-β {P}eptide {I}nteractions with {A}mphiphilic
                      {S}urfactants: {E}lectrostatic and {H}ydrophobic {E}ffects},
      journal      = {ACS chemical neuroscience},
      volume       = {9},
      number       = {7},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2018-07744},
      pages        = {1680 - 1692},
      year         = {2018},
      abstract     = {The amphiphilic nature of the amyloid-β (Aβ) peptide
                      associated with Alzheimer's disease facilitates various
                      interactions with biomolecules such as lipids and proteins,
                      with effects on both structure and toxicity of the peptide.
                      Here, we investigate these peptide-amphiphile interactions
                      by experimental and computational studies of Aβ(1-40) in
                      the presence of surfactants with varying physicochemical
                      properties. Our findings indicate that electrostatic
                      peptide-surfactant interactions are required for
                      coclustering and structure induction in the peptide and that
                      the strength of the interaction depends on the surfactant
                      net charge. Both aggregation-prone peptide-rich coclusters
                      and stable surfactant-rich coclusters can form. Only
                      Aβ(1-40) monomers, but not oligomers, are inserted into
                      surfactant micelles in this surfactant-rich state.
                      Surfactant headgroup charge is suggested to be important as
                      electrostatic peptide-surfactant interactions on the
                      micellar surface seems to be an initiating step toward
                      insertion. Thus, no peptide insertion or change in peptide
                      secondary structure is observed using a nonionic surfactant.
                      The hydrophobic peptide-surfactant interactions instead
                      stabilize the Aβ monomer, possibly by preventing
                      self-interaction between the peptide core and C-terminus,
                      thereby effectively inhibiting the peptide aggregation
                      process. These findings give increased understanding
                      regarding the molecular driving forces for Aβ aggregation
                      and the peptide interaction with amphiphilic biomolecules.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29683649},
      UT           = {WOS:000439531400017},
      doi          = {10.1021/acschemneuro.8b00065},
      url          = {https://juser.fz-juelich.de/record/858908},
}