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@ARTICLE{Vitiello:1034425,
      author       = {Vitiello, Giuseppe and Luchini, Alessandra and Di Napoli,
                      Michela and Gallucci, Noemi and Cavasso, Domenico and
                      Koutsioumpas, Alexandros and Varcamonti, Mario and
                      Zanfardino, Anna and Fragneto, Giovanna and Paduano, Luigi},
      title        = {{T}he affinity towards the hydrophobic region of
                      biomimicking bacterial membranes drives the antimicrobial
                      activity of {EFV}12 peptide from {L}actobacillus gasseri gut
                      microbiota},
      journal      = {Journal of molecular liquids},
      volume       = {414},
      number       = {Part A},
      issn         = {0167-7322},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2024-07206},
      pages        = {126086 -},
      year         = {2024},
      abstract     = {The gut microbiota consists of a large variety of
                      microorganisms, which interact with the immune system and
                      exert essential roles for the human body health. Many of
                      these microorganisms are also capable of producing various
                      bioactive molecules, such as selective antimicrobial
                      peptides, thus promoting the proliferation of only certain
                      bacterial strains. These result in the shaping of the
                      composition of the local microbiome and the co-evolution
                      with a complex microbiome. Recently, a small peptide, named
                      EFV12 and deriving from the bacterium Lactobacillus gasseri
                      SF1109 regularly placed in the human intestine, showed a
                      significant antimicrobial activity. Here we discuss a
                      biophysical study on the structural changes induced by the
                      peptide on lipid bilayers mimicking bacterial membranes with
                      the aim of shedding light on the molecular features driving
                      the biocidal activity against Gram(+) and Gram(−) strains.
                      Supported Lipid Bilayers and liposomes composed of
                      1,2-oleoyl-sn-glycero-3-phosphocholine and
                      1,2-oleoyl-sn-glycero-3-rac-phosphoglycerol, both in the
                      absence and presence of cardiolipin and lipopolysaccharides
                      (LPSs), were selected to investigate the peptide-lipid
                      interactions through a combination of specular Neutron
                      Reflectometry, Dynamic Light Scattering, Small-Angle X-ray
                      Scattering and Circular Dichroism measurements. The obtained
                      results indicated association of EFV12 peptide with the
                      hydrophobic region of lipid bilayers, which caused their
                      destabilization, and is thus driving the antimicrobial
                      activity against bacterial cells.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)MARIA-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1016/j.molliq.2024.126086},
      url          = {https://juser.fz-juelich.de/record/1034425},
}