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@ARTICLE{DiSomma:889023,
      author       = {Di Somma, Angela and Avitabile, Concetta and Cirillo,
                      Arianna and Moretta, Antonio and Merlino, Antonello and
                      Paduano, Luigi and Duilio, Angela and Romanelli, Alessandra},
      title        = {{T}he antimicrobial peptide {T}emporin {L} impairs {E}.
                      coli cell division by interacting with {F}ts{Z} and the
                      divisome complex},
      journal      = {Biochimica et biophysica acta / General subjects},
      volume       = {1864},
      number       = {7},
      issn         = {0304-4165},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2020-05396},
      pages        = {129606},
      year         = {2020},
      abstract     = {BackgroundThe comprehension of the mechanism of action of
                      antimicrobial peptides is fundamental for the design of new
                      antibiotics. Studies performed looking at the interaction of
                      peptides with bacterial cells offer a faithful picture of
                      what really happens in nature.MethodsIn this work we focused
                      on the interaction of the peptide Temporin L with E. coli
                      cells, using a variety of biochemical and biophysical
                      techniques that include: functional proteomics, docking,
                      optical microscopy, TEM, DLS, SANS, fluorescence.ResultsWe
                      identified bacterial proteins specifically interacting with
                      the peptides that belong to the divisome machinery; our data
                      suggest that the GTPase FtsZ is the specific peptide target.
                      Docking experiments supported the FtsZ-TL interaction;
                      binding and enzymatic assays using recombinant FtsZ
                      confirmed this hypothesis and revealed a competitive
                      inhibition mechanism. Optical microscopy and TEM
                      measurements demonstrated that, upon incubation with the
                      peptide, bacterial cells are unable to divide forming long
                      necklace-like cell filaments. Dynamic light scattering
                      studies and Small Angle Neutron Scattering experiments
                      performed on treated and untreated bacterial cells,
                      indicated a change at the nanoscale level of the bacterial
                      membrane.ConclusionsThe peptide temporin L acts by a
                      non-membrane-lytic mechanism of action, inhibiting the
                      divisome machinery.},
      cin          = {JCNS-FRM-II / MLZ},
      ddc          = {610},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32229224},
      UT           = {WOS:000536132200017},
      doi          = {10.1016/j.bbagen.2020.129606},
      url          = {https://juser.fz-juelich.de/record/889023},
}