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Delivery of membrane proteins into small and giant unilamellar vesicles by charge‐mediated fusion
Author(s) -
Biner Olivier,
Schick Thomas,
Müller Yannic,
Ballmoos Christoph
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12233
Subject(s) - liposome , lipid bilayer fusion , vesicle , lipid bilayer , membrane , membrane protein , escherichia coli , chemistry , biophysics , fusion protein , lipid vesicle , fusion , peripheral membrane protein , biochemistry , recombinant dna , biology , integral membrane protein , linguistics , philosophy , gene
One of the current challenges in synthetic biology is the production of stable membrane mimetic systems and the insertion of components in these systems. Here, we employ fusion of oppositely charged liposomes to deliver separately reconstituted membrane proteins into a common lipid bilayer. After a systematic evaluation of different lipid compositions by lipid mixing and size distribution analysis, suitable conditions were further investigated for proteoliposome fusion. With this technique, we functionally coreconstituted bo 3 oxidase and ATP synthase from Escherichia coli into unilamellar liposomes ranging from 100 nm to 50 μm in size. The presented method is a simple and versatile tool for oriented membrane protein reconstitution to produce biomimetic systems with increased complexity.