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@ARTICLE{Fenz:3462,
      author       = {Fenz, S.F. and Merkel, R. and Sengupta, K.},
      title        = {{D}iffusion and {I}ntermembrane {D}istance: {C}ase {S}tudy
                      of {A}vidin and {E}-{C}adherin {M}ediated {A}dhesion},
      journal      = {Langmuir},
      volume       = {25},
      issn         = {0743-7463},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {PreJuSER-3462},
      pages        = {1074 - 1085},
      year         = {2009},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {We present a biomimetic model system for cell-cell adhesion
                      consisting of a giant unilamellar vesicle (GUV) adhering via
                      specific ligand-receptor interactions to a supported lipid
                      bilayer (SLB). The modification of in-plane diffusion of
                      tracer lipids and receptors in the SLB membrane due to
                      adhesion to the GUV is reported. Adhesion was mediated by
                      either biotin-neutravidin (an avidin analogue) or the
                      extracellular domains of the cell adhesion molecule
                      E-cadherin (Ecad). In the strong interaction (biotin-avidin)
                      case, binding of soluble receptors to the SLB alone led to
                      reduced diffusion of tracer lipids. From theoretical
                      considerations, this could be attributed partially to
                      introduction of obstacles and partially to viscous effects.
                      Further specific binding of a GUV membrane caused additional
                      slowing down of tracers (up to $15\%)$ and immobilization of
                      receptors, and led to accumulation of receptors in the
                      adhesion zone until full coverage was achieved. The
                      intermembrane distance was measured to be 7 nm from
                      microinterferometry (RICM). We show that a crowding effect
                      due to the accumulated receptors alone is not sufficient to
                      account for the slowing downan additional friction from the
                      membrane also plays a role. In the weak binding case (Ecad),
                      the intermembrane distance was about 50 nm, corresponding to
                      partial overlap of the Ecad domains. No significant change
                      in diffusion of tracer lipids was observed upon either
                      protein binding or subsequent vesicle binding. The former
                      was probably due to very small effective size of the
                      obstacles introduced into the bilayer by Ecad binding,
                      whereas the latter was due to the fact that, with such high
                      intermembrane distance, the resulting friction is
                      negligible. We conclude that the effect of intermembrane
                      adhesion on diffusion depends strongly on the choice of the
                      receptors.},
      keywords     = {Avidin: chemistry / Binding Sites / Biomimetic Materials:
                      chemistry / Cadherins: chemistry / Diffusion / Lipid
                      Bilayers: chemistry / Surface Properties / Cadherins (NLM
                      Chemicals) / Lipid Bilayers (NLM Chemicals) / neutravidin
                      (NLM Chemicals) / Avidin (NLM Chemicals) / J (WoSType)},
      cin          = {IBN-4},
      ddc          = {670},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Chemistry, Multidisciplinary / Chemistry, Physical /
                      Materials Science, Multidisciplinary},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19072315},
      UT           = {WOS:000262431100061},
      doi          = {10.1021/la803227s},
      url          = {https://juser.fz-juelich.de/record/3462},
}