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@ARTICLE{Majewski:89041,
      author       = {Majewski, J. and Stec, B. and DESY},
      title        = {{X}-ray scattering studies of model lipid membrane
                      interacting with purothionin provide support for a
                      previously proposed mechanism of membrane lysis},
      journal      = {European biophysics journal},
      volume       = {39},
      issn         = {0175-7571},
      address      = {Berlin},
      publisher    = {Springer},
      reportid     = {PHPPUBDB-16564},
      pages        = {1155},
      year         = {2009},
      note         = {(c) European Biophysical Societies’ Association ; Post
                      referee fulltext in progress 2; Embargo 12 months from
                      publication},
      abstract     = {Thionins, ubiquitous plant toxins, are believed to act by
                      lysing the membrane of pathogenic organisms. Several
                      competing mechanisms were proposed for the lysis of
                      phospholipid membranes by the toxins. In order to study in
                      more detail the proposed mechanisms and possibly resolve
                      among the competing proposals, the interactions of
                      purothionins with a model lipid membrane in the form of a
                      monolayer were studied. The monolayer formed at the
                      air-water interface was studied by synchrotron X-ray
                      reflectivity and grazing incidents diffraction methods. The
                      model membrane was composed of 90:10 $mol\%$ DPPC:DPPS
                      (dipylmitoyl phosphatidylcholine:dipylmitoyl
                      phosphatidylserine). The protein interaction with the
                      monolayer disturbs the in-plane and out-of-plane order of
                      phospholipids, increases the amount of the liquid phase of
                      the monolayer, and increases the average surface area per
                      alkyl chain. The results indicate that the protein is bound
                      only transiently, and after approximately 4 h most of the
                      properties of the monolayer are reminiscent of the pure DPPC
                      monolayer suggesting partial withdrawal of DPPS. Obtained
                      electron density distributions perpendicular to the membrane
                      interface do not show any significant contribution from the
                      adsorbed proteins, further supporting the withdrawal
                      hypothesis.},
      keywords     = {1,2-Dipalmitoylphosphatidylcholine: chemistry / Air /
                      Antimicrobial Cationic Peptides: chemistry / Cell Membrane:
                      chemistry / Cell Membrane: physiology / Electrons / Kinetics
                      / Membranes, Artificial / Models, Chemical /
                      Phosphatidylserines: chemistry / Phospholipids: chemistry /
                      Plant Proteins: chemistry / Scattering, Radiation /
                      Synchrotrons / Unilamellar Liposomes: chemistry / Water /
                      X-Ray Diffraction / X-Rays / Antimicrobial Cationic Peptides
                      (NLM Chemicals) / Membranes, Artificial (NLM Chemicals) /
                      Phosphatidylserines (NLM Chemicals) / Phospholipids (NLM
                      Chemicals) / Plant Proteins (NLM Chemicals) / Unilamellar
                      Liposomes (NLM Chemicals) /
                      1,2-Dipalmitoylphosphatidylcholine (NLM Chemicals) /
                      dipalmitoylphosphatidylserine (NLM Chemicals) / Water (NLM
                      Chemicals) / purothionin (NLM Chemicals)},
      cin          = {HASYLAB(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)HASYLAB_-2012_-20130307$},
      pnm          = {DORIS Beamline BW1 (POF1-550) / DORIS Beamline E2
                      (POF1-550)},
      pid          = {G:(DE-H253)POF1-BW1-20130405 / G:(DE-H253)POF1-E2-20130405},
      experiment   = {EXP:(DE-H253)D-BW1-20150101 / EXP:(DE-H253)D-E2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19997910},
      UT           = {WOS:000279194500005},
      doi          = {10.1007/s00249-009-0568-0},
      url          = {https://bib-pubdb1.desy.de/record/89041},
}