% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Pachler:867574,
      author       = {Pachler, Michael and Kabelka, Ivo and Appavou, Marie-Sousai
                      and Lohner, Karl and Vácha, Robert and Pabst, Georg},
      title        = {{M}againin 2 and {PGL}a in {B}acterial {M}embrane {M}imics
                      {I}: {P}eptide-{P}eptide and {L}ipid-{P}eptide
                      {I}nteractions},
      journal      = {Biophysical journal},
      volume       = {117},
      number       = {10},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2019-06197},
      pages        = {1858 - 1869},
      year         = {2019},
      abstract     = {We addressed the onset of synergistic activity of the two
                      well-studied antimicrobial peptides magainin 2 (MG2a) and
                      PGLa using lipid-only mimics of Gram-negative cytoplasmic
                      membranes. Specifically, we coupled a joint analysis of
                      small-angle x-ray and neutron scattering experiments on
                      fully hydrated lipid vesicles in the presence of MG2a and
                      L18W-PGLa to all-atom and coarse-grained molecular dynamics
                      simulations. In agreement with previous studies, both
                      peptides, as well as their equimolar mixture, were found to
                      remain upon adsorption in a surface-aligned topology and to
                      induce significant membrane perturbation, as evidenced by
                      membrane thinning and hydrocarbon order parameter changes in
                      the vicinity of the inserted peptide. These effects were
                      particularly pronounced for the so-called synergistic
                      mixture of 1:1 (mol/mol) L18W-PGLa/MG2a and cannot be
                      accounted for by a linear combination of the membrane
                      perturbations of two peptides individually. Our data are
                      consistent with the formation of parallel heterodimers at
                      concentrations below a synergistic increase of dye leakage
                      from vesicles. Our simulations further show that the
                      heterodimers interact via salt bridges and hydrophobic
                      forces, which apparently makes them more stable than
                      putatively formed antiparallel L18W-PGLa and MG2a
                      homodimers. Moreover, dimerization of L18W-PGLa and MG2a
                      leads to a relocation of the peptides within the lipid
                      headgroup region as compared to the individual peptides. The
                      early onset of dimerization of L18W-PGLa and MG2a at low
                      peptide concentrations consequently appears to be key to
                      their synergistic dye-releasing activity from lipid vesicles
                      at high concentrations},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / 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)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31703802},
      UT           = {WOS:000497815800009},
      doi          = {10.1016/j.bpj.2019.10.022},
      url          = {https://juser.fz-juelich.de/record/867574},
}