Langton, M.J. orcid.org/0000-0003-1555-3479, Williams, N.H. and Hunter, C.A. orcid.org/0000-0002-5182-1859 (2017) Recognition-Controlled Membrane Translocation for Signal Transduction across Lipid Bilayers. Journal of the American Chemical Society, 139 (18). pp. 6461-6466. ISSN 0002-7863
Abstract
Membrane signaling proteins transduce information across lipid bilayer membranes in response to extra-cellular binding of chemical messengers. The design of chemical systems that initiate transmembrane signal transduction through molecular binding events is a critical step toward preparing responsive synthetic vesicles. Here we report a vesicle-based signaling system controlled by a metal cation binding event. Competition between binding of copper ions to a membrane-embedded synthetic transducer and to an extra-vesicle messenger (EDTA) is used to control translocation of the transducer across the lipid bilayer. The translocation process is coupled to activation of a catalyst that turns over encapsulated substrates on the inside of the vesicle to generate an amplified fluorescence output signal. External EDTA and copper ions can be used to reversibly switch catalysis inside the vesicles on and off in a controlled manner.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2017 American Chemical Society. ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 17 May 2017 15:38 |
Last Modified: | 03 May 2018 00:39 |
Published Version: | https://doi.org/10.1021/jacs.7b02345 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1021/jacs.7b02345 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:116503 |