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@ARTICLE{GhoshMoulick:820386,
      author       = {Ghosh Moulick, R. and Afanasenkau, D. and Choi, S.-E. and
                      Albers, J. and Lange, W. and Maybeck, V. and Utesch, T. and
                      Offenhäusser, Andreas},
      title        = {{R}econstitution of {F}usion {P}roteins in {S}upported
                      {L}ipid {B}ilayers for the {S}tudy of {C}ell {S}urface
                      {R}eceptor–{L}igand {I}nteractions in {C}ell–{C}ell
                      {C}ontact},
      journal      = {Langmuir},
      volume       = {32},
      number       = {14},
      issn         = {1520-5827},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2016-05717},
      pages        = {3462 - 3469},
      year         = {2016},
      abstract     = {Bioactive molecules such as adhesion ligands, growth
                      factors, or enzymes play an important role in modulating
                      cell behavior such as cell adhesion, spreading, and
                      differentiation. Deciphering the mechanism of
                      ligand-mediated cell adhesion and associated signaling is of
                      great interest not only for fundamental biophysical
                      investigations but also for applications in medicine and
                      biotechnology. In the presented work, we developed a new
                      biomimetic platform that enables culturing primary neurons
                      and testing cell surface–receptor ligand interactions in
                      cell–cell contacts as, e.g., in neuronal synapses. This
                      platform consists of a supported lipid bilayer modified with
                      incorporated neuronal adhesion proteins conjugated with the
                      Fc-domain of IgG (ephrin A5 Fc-chimera). We extensively
                      characterized properties of these protein containing
                      bilayers using fluorescence recovery after photobleaching
                      (FRAP), quartz crystal microbalance with dissipation
                      (QCM-D), and immunostaining. We conclude that the Fc-domain
                      is the part responsible for the incorporation of the protein
                      into the bilayer. The biomimetic platform prepared by this
                      new approach was able to promote neuronal cell adhesion and
                      maintain growth as well as facilitate neuronal maturation as
                      shown by electrophysiological measurements. We believe that
                      our approach can be extended to insert other proteins to
                      create a general culture platform for neurons and other cell
                      types.},
      cin          = {ICS-8},
      ddc          = {670},
      cid          = {I:(DE-Juel1)ICS-8-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552) / GRK 1572 -
                      Bionik - Interaktionen über Grenzflächen zur Außenwelt
                      (90190939)},
      pid          = {G:(DE-HGF)POF3-552 / G:(GEPRIS)90190939},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000374196700016},
      pubmed       = {pmid:26986674},
      doi          = {10.1021/acs.langmuir.5b04644},
      url          = {https://juser.fz-juelich.de/record/820386},
}