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@ARTICLE{Silva:418100,
      author       = {Silva, Tânia and Claro, Bárbara and Silva, Bruno F. B.
                      and Vale, Nuno and Gomes, Paula and Gomes, Maria Salomé and
                      Funari, Sergio de Souza and Teixeira, José and Uhríková,
                      Daniela and Bastos, Margarida},
      title        = {{U}nravelling a {M}echanism of {A}ction for a {C}ecropin
                      {A}-{M}elittin {H}ybrid {A}ntimicrobial {P}eptide: {T}he
                      {I}nduced {F}ormation of {M}ultilamellar {L}ipid {S}tacks},
      journal      = {Langmuir},
      volume       = {34},
      number       = {5},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {PUBDB-2019-00187},
      pages        = {2158 - 2170},
      year         = {2018},
      note         = {© American Chemical Society},
      abstract     = {An understanding of the mechanism of action of
                      antimicrobial peptides is fundamental to the development of
                      new and more active antibiotics. In the present work, we use
                      a wide range of techniques (SANS, SAXD, DSC, ITC, CD, and
                      confocal and electron microscopy) in order to fully
                      characterize the interaction of a cecropin A-melittin hybrid
                      antimicrobial peptide, CA(1-7)M(2-9), of known antimicrobial
                      activity, with a bacterial model membrane of POPE/POPG in an
                      effort to unravel its mechanism of action. We found that
                      CA(1-7)M(2-9) disrupts the vesicles, inducing membrane
                      condensation and forming an onionlike structure of
                      multilamellar stacks, held together by the intercalated
                      peptides. SANS and SAXD revealed changes induced by the
                      peptide in the lipid bilayer thickness and the bilayer
                      stiffening in a tightly packed liquid-crystalline lamellar
                      phase. The analysis of the observed abrupt changes in the
                      repeat distance upon the phase transition to the gel state
                      suggests the formation of an L$_γ$ phase. To the extent of
                      our knowledge, this is the first time that the $_γ$ phase
                      is identified as part of the mechanism of action of
                      antimicrobial peptides. The energetics of interaction
                      depends on temperature, and ITC results indicate that
                      CA(1-7)M(2-9) interacts with the outer leaflet. This further
                      supports the idea of a surface interaction that leads to
                      membrane condensation and not to pore formation. As a
                      result, we propose that this peptide exerts its
                      antimicrobial action against bacteria through extensive
                      membrane disruption that leads to cell death.},
      cin          = {DOOR / FS-PEX},
      ddc          = {540},
      cid          = {I:(DE-H253)HAS-User-20120731 / I:(DE-H253)FS-PEX-20130206},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-H253)D-A2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29304549},
      UT           = {WOS:000424730500037},
      doi          = {10.1021/acs.langmuir.7b03639},
      url          = {https://bib-pubdb1.desy.de/record/418100},
}