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@ARTICLE{Brandenburg:317044,
      author       = {Brandenburg, Klaus and Heinbockel, Lena and Correa, Wilmar
                      and Fukuoka, Satoshi and Gutsmann, Thomas and Zähringer,
                      Ulrich and Koch, Michel H. J.},
      title        = {{S}upramolecular structure of enterobacterial wild-type
                      lipopolysaccharides ({LPS}), fractions thereof, and their
                      neutralization by {P}ep19-2.5},
      journal      = {Journal of structural biology},
      volume       = {194},
      number       = {1},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2017-00385},
      pages        = {68 - 77},
      year         = {2016},
      note         = {© Elsevier Inc},
      abstract     = {Lipopolysaccharides (LPS) belong to the strongest
                      immune-modulating compounds known in nature, and are often
                      described as pathogen-associated molecular patterns (PAMPs).
                      In particular, at higher concentrations they are responsible
                      for sepsis and the septic shock syndrome associated with
                      high lethality. Since most data are indicative that LPS
                      aggregates are the bioactive units, their supramolecular
                      structures are considered to be of outmost relevance for
                      deciphering the molecular mechanisms of its bioactivity. So
                      far, however, most of the data available addressing this
                      issue, were published only for the lipid part (lipid A) and
                      the core-oligosaccharide containing rough LPS, representing
                      the bioactive unit. By contrast, it is well known that most
                      of the LPS specimen identified in natural habitats contain
                      the smooth-form (S-form) LPS, which carry additionally a
                      high-molecular polysaccharide (O-chain). To fill this lacuna
                      and going into a more natural system, here various wild-type
                      (smooth form) LPS including also some LPS fractions were
                      investigated by small-angle X-ray scattering with
                      synchrotron radiation to analyze their aggregate structure.
                      Furthermore, the influence of a recently designed synthetic
                      anti-LPS peptide (SALP) Pep19-2.5 on the aggregate
                      structure, on the binding thermodynamics, and on the
                      cytokine-inducing activity of LPS were characterized,
                      showing defined aggregate changes, high affinity binding and
                      inhibition of cytokine secretion. The data obtained are
                      suitable to refine our view on the preferences of LPS for
                      non-lamellar structures, representing the highest bioactive
                      forms which can be significantly influenced by the binding
                      with neutralizing peptides such as Pep19-2.5.},
      cin          = {EMBL},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000371193600008},
      pubmed       = {pmid:26828112},
      doi          = {10.1016/j.jsb.2016.01.014},
      url          = {https://bib-pubdb1.desy.de/record/317044},
}