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Fusion Domains Guide the Oriented Insertion of Light-Driven Proton Pumps into Liposomes

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Ritzmann Noah, Thoma Johannes, Hirschi Stephan, Kalbermatter David, Fotiadis Dimitrios, Müller Daniel J.,
Project Structure and supramolecular organization of membrane transport proteins
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Original article (peer-reviewed)

Journal Biophysical Journal
Volume (Issue) 113(6)
Page(s) 1181 - 1186
Title of proceedings Biophysical Journal
DOI 10.1016/j.bpj.2017.06.022


One major objective of synthetic biology is the bottom-up assembly of minimalistic nanocells consisting of lipid or polymer vesicles as architectural scaffolds and of membrane and soluble proteins as functional elements. However, there is no reliable method to orient membrane proteins reconstituted into vesicles. Here, we introduce a simple approach to orient the insertion of the light-driven proton pump proteorhodopsin (PR) into liposomes. To this end, we engineered red or green fluorescent proteins to the N- or C-terminus of PR, respectively. The fluorescent proteins optically identified the PR constructs and guided the insertion of PR into liposomes with the unoccupied terminal end facing inward. Using the PR constructs, we generated proton gradients across the vesicle membrane along predefined directions such as are required to power (bio)chemical processes in nanocells. Our approach may be adapted to direct the insertion of other membrane proteins into vesicles.