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@ARTICLE{Fenz:15804,
      author       = {Fenz, S. and Smith, A.S. and Merkel, R. and Sengupta, K.},
      title        = {{I}nter-membrane adhesion mediated by mobile linkers:
                      {E}ffect of receptor shortage},
      journal      = {Soft matter},
      volume       = {7},
      issn         = {1744-683X},
      address      = {Cambridge},
      publisher    = {Royal Society of Chemistry (RSC)},
      reportid     = {PreJuSER-15804},
      pages        = {952 - 962},
      year         = {2011},
      note         = {A.-S. S. acknowledges funding by the Deutsche
                      Forschungsgemeinschaft DFG-SE 1119/2-1 and the Grant 22/08
                      of the Unity through Knowledge Fund, Croatia.},
      abstract     = {Giant unilamellar vesicles (GUVs) adhering to supported
                      bilayers were used as a model system to mimic
                      ligand-receptor mediated cell-cell adhesion. We present the
                      effect of varying the concentration of receptors
                      (neutravidin on the bilayer) and ligands (biotin on the
                      vesicle) on GUV adhesion and the organization of receptors
                      in the adhesion zone. At high concentrations of both ligands
                      and receptors, the adhesion is strong, all the available
                      membrane is adhered and receptors are accumulated under the
                      adhered membrane up to the geometrical limit of close
                      packing. At low concentrations of receptors $(<0.5\%),$ and
                      an arbitrary concentration of ligands (>= $0.1\%),$ adhesion
                      does not proceed to completion: the membrane is only
                      partially bound and parts of it still fluctuate. The
                      receptors tend to accumulate under the adhered membrane but
                      the filling is partial. Receptors get jammed and form
                      clusters with fractal like shapes along the rim of the
                      adhered vesicle in such a way that the annular cluster
                      prevents further filling of the adhesion disc. We
                      characterize the filling in terms of a compaction factor and
                      the final concentration. Interestingly, the closing of the
                      ring of jammed clusters switches the interior of the
                      adhesion disc from one thermodynamic ensemble to another. In
                      the new ensemble the receptors sealed within the adhesion
                      disc are mobile but their number is fixed. Under such
                      conditions, the usually strong neutravidin/biotin bond is
                      weak. The incomplete adhesion state can be attributed to a
                      combination of the effects of diffusion, jamming and the
                      competition of enthalpy and entropy on bond formation. The
                      formation of jammed receptor clusters reported here
                      represents a new mechanism that influences membrane
                      adhesion.},
      keywords     = {J (WoSType)},
      cin          = {ICS-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Chemistry, Physical / Materials Science, Multidisciplinary
                      / Physics, Multidisciplinary / Polymer Science},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000286615500023},
      doi          = {10.1039/c0sm00550a},
      url          = {https://juser.fz-juelich.de/record/15804},
}