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000010588 0247_ $$2pmid$$apmid:20355933
000010588 0247_ $$2DOI$$a10.1021/la1005242
000010588 0247_ $$2WOS$$aWOS:000279239900087
000010588 037__ $$aPreJuSER-10588
000010588 041__ $$aeng
000010588 082__ $$a670
000010588 084__ $$2WoS$$aChemistry, Multidisciplinary
000010588 084__ $$2WoS$$aChemistry, Physical
000010588 084__ $$2WoS$$aMaterials Science, Multidisciplinary
000010588 1001_ $$0P:(DE-Juel1)VDB5493$$aDieluweit, S.$$b0$$uFZJ
000010588 245__ $$aMechanical Properties of Bare and Protein-Coated Giant Unilamellar Phospolipid Vesicles. A Comparative Study of Micropipet Aspiration and Atomic Force Microscopy
000010588 260__ $$aWashington, DC$$bACS Publ.$$c2010
000010588 300__ $$a11041 - 11049
000010588 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000010588 440_0 $$04081$$aLangmuir$$v26$$x0743-7463$$y13
000010588 500__ $$aRecord converted from VDB: 12.11.2012
000010588 520__ $$aIn this study, protein-coated giant phospholipid vesicles were used to model cell plasma membranes coated by surface protein layers that increase membrane stiffness under mechanical or osmotic stress. These changed mechanical properties like bending stiffness, membrane area compressibility modulus, and effective Young's modulus were determined by micropipet aspiration, while bending stiffness, effective Young's modulus, and effective spring constant of vesicles were analyzed by AFM. The experimental setups, the applied models, and the results using both methods were compared here. As demonstrated before, we found that bare vesicles were best probed by micropipet aspiration due to its high sensitivity. The mechanical properties of vesicles with protein surface layers were, however, better determined by AFM because it enables very local deformations of the membrane with barely any structural damage to the protein layer. Mechanical properties of different species of coating proteins, here streptavidin and avidin, could be clearly distinguished using this technique.
000010588 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000010588 588__ $$aDataset connected to Web of Science, Pubmed
000010588 650_2 $$2MeSH$$aMechanics
000010588 650_2 $$2MeSH$$aMicroscopy, Atomic Force
000010588 650_2 $$2MeSH$$aModels, Theoretical
000010588 650_2 $$2MeSH$$aPhospholipids: chemistry
000010588 650_2 $$2MeSH$$aUnilamellar Liposomes: chemistry
000010588 650_7 $$00$$2NLM Chemicals$$aPhospholipids
000010588 650_7 $$00$$2NLM Chemicals$$aUnilamellar Liposomes
000010588 650_7 $$2WoSType$$aJ
000010588 7001_ $$0P:(DE-Juel1)128805$$aCsiszar, A.$$b1$$uFZJ
000010588 7001_ $$0P:(DE-Juel1)128837$$aRubner, W.$$b2$$uFZJ
000010588 7001_ $$0P:(DE-Juel1)VDB19661$$aFleischhauer, J.$$b3$$uFZJ
000010588 7001_ $$0P:(DE-Juel1)VDB87855$$aHouben, S.$$b4$$uFZJ
000010588 7001_ $$0P:(DE-Juel1)128833$$aMerkel, R.$$b5$$uFZJ
000010588 773__ $$0PERI:(DE-600)2005937-1$$a10.1021/la1005242$$gVol. 26, p. 11041 - 11049$$p11041 - 11049$$q26<11041 - 11049$$tLangmuir$$v26$$x0743-7463$$y2010
000010588 8567_ $$uhttp://dx.doi.org/10.1021/la1005242
000010588 909CO $$ooai:juser.fz-juelich.de:10588$$pVDB
000010588 9131_ $$0G:(DE-Juel1)FUEK505$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x0
000010588 9141_ $$y2010
000010588 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000010588 9201_ $$0I:(DE-Juel1)VDB802$$d31.12.2010$$gIBN$$kIBN-4$$lBiomechanik$$x0
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