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Reference: Ishmukhametov, R, Russell, AN and Berry, RM, (2016). A modular platform for one-step assembly of multi-component membrane systems by fusion of charged proteoliposomes. Nature Communications, 7, Article: 13025.Citable link to this page:

 

A modular platform for one-step assembly of multi-component membrane systems by fusion of charged proteoliposomes

Abstract: An important goal in synthetic biology is the assembly of biomimetic cell-like structures, which combine multiple biological components in synthetic lipid vesicles. A key limiting assembly step is the incorporation of membrane proteins into the lipid bilayer of the vesicles. Here we present a simple method for delivery of membrane proteins into a lipid bilayer within 5 min. Fusogenic proteoliposomes, containing charged lipids and membrane proteins, fuse with oppositely charged bilayers, with no requirement for detergent or fusion-promoting proteins, and deliver large, fragile membrane protein complexes into the target bilayers. We demonstrate the feasibility of our method by assembling a minimal electron transport chain capable of adenosine triphosphate (ATP) synthesis, combining Escherichia coli F1Fo ATP-synthase and the primary proton pump bo3-oxidase, into synthetic lipid vesicles with sizes ranging from 100 nm to ∼10 μm. This provides a platform for the combination of multiple sets of membrane protein complexes into cell-like artificial structures.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionDate of acceptance:25 August 2016Notes:This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

Bibliographic Details

Publisher: Nature Publishing Group

Publisher Website: http://www.nature.com/

Journal: Nature Communicationssee more from them

Publication Website: http://www.nature.com/ncomms

Volume: 7

Extent: Article: 13025

Issue Date: 06 October 2016

pages:Article: 13025Identifiers

Doi: https://doi.org/10.1038/ncomms13025

Issn: 2041-1723

Uuid: uuid:e6c2fd1b-1d72-416c-8d20-ce959d4fd5bd

Urn: uri:e6c2fd1b-1d72-416c-8d20-ce959d4fd5bd

Pubs-id: pubs:648241 Item Description

Type: journal-article;

Version: Publisher's version

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Author: Ishmukhametov, R - Oxford, MPLS, Physics, Condensed Matter Physics fundingBiotechnology and Biological Sciences Research Council

Source: https://ora.ox.ac.uk/objects/uuid:e6c2fd1b-1d72-416c-8d20-ce959d4fd5bd



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