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@ARTICLE{Nielsen:889770,
      author       = {Nielsen, Josefine Eilsø and Bjørnestad, Victoria Ariel
                      and Pipich, Vitaliy and Jenssen, Håvard and Lund, Reidar},
      title        = {{B}eyond structural models for the mode of action: {H}ow
                      natural antimicrobial peptides affect lipid transport},
      journal      = {Journal of colloid and interface science},
      volume       = {582},
      number       = {Part B},
      issn         = {0021-9797},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2021-00383},
      pages        = {793 - 802},
      year         = {2021},
      abstract     = {Hypothesis: Most textbook models for antimicrobial peptides
                      (AMP) mode of action are focused on structural effects and
                      pore formation in lipid membranes, while these deformations
                      have been shown to require high concentrations of peptide
                      bound to the membrane. Even insertion of low amounts of
                      peptides in the membrane is hypothesized to affect the
                      transmembrane transport of lipids, which may play a key role
                      in the peptide effect on membranes. Experiments: Here we
                      combine state-of-the-art small angle X-ray/neutron
                      scattering (SAXS/SANS) techniques to systematically study
                      the effect of a broad selection of natural AMPs on lipid
                      membranes. Our approach enables us to relate the structural
                      interactions, effects on lipid exchange processes, and
                      thermodynamic parameters, directly in the same model system.
                      Findings: The studied peptides, indolicidin, aurein 1.2,
                      magainin II, cecropin A and LL-37 all cause a general
                      acceleration of essential lipid transport processes, without
                      necessarily altering the overall structure of the lipid
                      membranes or creating organized pore-like structures. We
                      observe rapid scrambling of the lipid composition associated
                      with enhanced lipid transport which may trigger lethal
                      signaling processes and enhance ion transport. The reported
                      membrane effects provide a plausible canonical mechanism of
                      AMP-membrane interaction and can reconcile many of the
                      previously observed effects of AMPs on bacterial membranes.},
      cin          = {JCNS-4 / JCNS-1 / JCNS-FRM-II / MLZ},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-4-20201012 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (FZJ) (POF4-6G4) / 632 - Materials
                      – Quantum, Complex and Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF4-6G4 /
                      G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32911421},
      UT           = {WOS:000600666100002},
      doi          = {10.1016/j.jcis.2020.08.094},
      url          = {https://juser.fz-juelich.de/record/889770},
}