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000003462 0247_ $$2pmid$$apmid:19072315
000003462 0247_ $$2DOI$$a10.1021/la803227s
000003462 0247_ $$2WOS$$aWOS:000262431100061
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000003462 041__ $$aeng
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000003462 084__ $$2WoS$$aChemistry, Multidisciplinary
000003462 084__ $$2WoS$$aChemistry, Physical
000003462 084__ $$2WoS$$aMaterials Science, Multidisciplinary
000003462 1001_ $$0P:(DE-Juel1)VDB84049$$aFenz, S.F.$$b0$$uFZJ
000003462 245__ $$aDiffusion and Intermembrane Distance: Case Study of Avidin and E-Cadherin Mediated Adhesion
000003462 260__ $$aWashington, DC$$bACS Publ.$$c2009
000003462 300__ $$a1074 - 1085
000003462 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000003462 440_0 $$04081$$aLangmuir$$v25$$x0743-7463$$y2
000003462 500__ $$aRecord converted from VDB: 12.11.2012
000003462 520__ $$aWe 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.
000003462 536__ $$0G:(DE-Juel1)FUEK414$$2G:(DE-HGF)$$aKondensierte Materie$$cP54$$x0
000003462 588__ $$aDataset connected to Web of Science, Pubmed
000003462 650_2 $$2MeSH$$aAvidin: chemistry
000003462 650_2 $$2MeSH$$aBinding Sites
000003462 650_2 $$2MeSH$$aBiomimetic Materials: chemistry
000003462 650_2 $$2MeSH$$aCadherins: chemistry
000003462 650_2 $$2MeSH$$aDiffusion
000003462 650_2 $$2MeSH$$aLipid Bilayers: chemistry
000003462 650_2 $$2MeSH$$aSurface Properties
000003462 650_7 $$00$$2NLM Chemicals$$aCadherins
000003462 650_7 $$00$$2NLM Chemicals$$aLipid Bilayers
000003462 650_7 $$00$$2NLM Chemicals$$aneutravidin
000003462 650_7 $$01405-69-2$$2NLM Chemicals$$aAvidin
000003462 650_7 $$2WoSType$$aJ
000003462 7001_ $$0P:(DE-Juel1)128833$$aMerkel, R.$$b1$$uFZJ
000003462 7001_ $$0P:(DE-Juel1)VDB57655$$aSengupta, K.$$b2$$uFZJ
000003462 773__ $$0PERI:(DE-600)2005937-1$$a10.1021/la803227s$$gVol. 25, p. 1074 - 1085$$p1074 - 1085$$q25<1074 - 1085$$tLangmuir$$v25$$x0743-7463$$y2009
000003462 8567_ $$uhttp://dx.doi.org/10.1021/la803227s
000003462 909CO $$ooai:juser.fz-juelich.de:3462$$pVDB
000003462 9131_ $$0G:(DE-Juel1)FUEK414$$bMaterie$$kP54$$lKondensierte Materie$$vKondensierte Materie$$x0$$zentfällt   bis 2009
000003462 9141_ $$y2009
000003462 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000003462 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
000003462 970__ $$aVDB:(DE-Juel1)109501
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000003462 981__ $$aI:(DE-Juel1)IBI-2-20200312
000003462 981__ $$aI:(DE-Juel1)ICS-7-20110106