Langton, M.J., Keymeulen, F., Ciaccia, M. et al. (2 more authors) (2016) Controlled membrane translocation provides a mechanism for signal transduction and amplification. Nature Chemistry. ISSN 1755-4330
Abstract
Transmission and amplification of chemical signals across lipid bilayer membranes is of profound significance in many biological processes, from the development of multi-cellular organisms to information processing in the nervous system. In biology, membrane-spanning proteins are responsible for transmission of chemical signals across membranes, and signal transduction is often associated with an amplified signaling cascade. The ability to reproduce such processes in artificial systems has potential applications in sensing, controlled drug delivery and communication between compartments in tissue-like constructs of synthetic vesicles. Here we describe a new mechanism for transmitting chemical signals across membranes based on controlled translocation of a synthetic molecular transducer from one side of a lipid bilayer membrane to the other. The controlled molecular motion has been coupled to activation of a catalyst on the inside of a vesicle, which leads to a signal amplification process analogous to the biological counterpart.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 Nature Publishing. This is an author produced version of a paper subsequently published in Nature Chemistry. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Membranes; Nanoscale devices; Supramolecular chemistry |
Dates: |
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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: | 02 Feb 2017 15:10 |
Last Modified: | 18 Jul 2017 12:50 |
Published Version: | https://doi.org/10.1038/nchem.2678 |
Status: | Published |
Publisher: | Nature Publishing Group |
Refereed: | Yes |
Identification Number: | 10.1038/nchem.2678 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:111255 |