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Search: id:"swepub:oai:research.chalmers.se:74d884eb-182e-42c6-91a0-a52d936e71fe" > Preserved Transmemb...

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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004032naa a2200397 4500
001oai:research.chalmers.se:74d884eb-182e-42c6-91a0-a52d936e71fe
003SwePub
008171008s2015 | |||||||||||000 ||eng|
0247 a https://doi.org/10.1021/acs.analchem.5b014492 DOI
0247 a https://research.chalmers.se/publication/2234342 URI
040 a (SwePub)cth
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Pace, Hudson,d 1982u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)hudsonp
2451 0a Preserved Transmembrane Protein Mobility in Polymer-Supported Lipid Bilayers Derived from Cell Membranes
264 c 2015-08-24
264 1b American Chemical Society (ACS),c 2015
520 a Supported lipid bilayers (SLBs) have contributed invaluable information about the physiochemical properties of cell membranes, but their compositional simplicity often limits the level of knowledge that can be gained about the structure and function of transmembrane proteins in their native environment. Herein, we demonstrate a generic protocol for producing polymer-supported lipid bilayers on glass surfaces that contain essentially all naturally occurring cell-membrane components of a cell line while still retaining transmembrane protein mobility and activity. This was achieved by merging vesicles made from synthetic lipids (PEGylated lipids and POPC lipids) with native cell-membrane vesicles to generate hybrid vesicles which readily rupture into a continuous polymer-supported lipid bilayer. To investigate the properties of these complex hybrid SLBs and particularly the behavior of their integral membrane-proteins, we used total internal reflection fluorescence imaging to study a transmembrane protease, β-secretase 1 (BACE1), whose ectoplasmic and cytoplasmic domains could both be specifically targeted with fluorescent reporters. By selectively probing the two different orientations of BACE1 in the resulting hybrid SLBs, the role of the PEG-cushion on transmembrane protein lateral mobility was investigated. The results reveal the necessity of having the PEGylated lipids present during vesicle adsorption to prevent immobilization of transmembrane proteins with protruding domains. The proteolytic activity of BACE1 was unadulterated by the sonication process used to merge the synthetic and native membrane vesicles; importantly it was also conserved in the SLB. The presented strategy could thus serve both fundamental studies of membrane biophysics and the production of surface-based bioanalytical sensor platforms.
650 7a NATURVETENSKAPx Biologix Cellbiologi0 (SwePub)106042 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Cell Biology0 (SwePub)106042 hsv//eng
650 7a NATURVETENSKAPx Biologix Biofysik0 (SwePub)106032 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biophysics0 (SwePub)106032 hsv//eng
7001 a Simonsson Nyström, Lisa,d 1982u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)slisa
7001 a Gunnarsson, Anders,d 1981u AstraZeneca AB4 aut0 (Swepub:cth)kb01guan
7001 a Eck, Elizabeth,d 1982u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)eeke
7001 a Monson, C.u Southern Utah University4 aut
7001 a Geschwindner, S.u AstraZeneca AB4 aut
7001 a Snijder, Arjan,d 1971u AstraZeneca AB4 aut
7001 a Höök, Fredrik,d 1966u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)fredrikh
7102 a Chalmers tekniska högskolab AstraZeneca AB4 org
7730 t Analytical Chemistryd : American Chemical Society (ACS)g 87:18, s. 9194-9203q 87:18<9194-9203x 0003-2700x 1520-6882
8564 u http://dx.doi.org/10.1021/acs.analchem.5b01449y FULLTEXT
8564 8u https://doi.org/10.1021/acs.analchem.5b01449
8564 8u https://research.chalmers.se/publication/223434

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