Outer membrane mimics using novel thiol-PC

DOI

We have recently shown that dense monolayers of PC can be assembled on gold surfaces using a new omega thiol PC from Avanti. This has two advantages over our previous methods. Firstly for outer membrane mimics assembled directly on the surface we now have a single layer with PC head groups facing the solution whereas before we needed two layers. We can incorporate outer membrane proteins into this layer and observe their protein-protein interactions with antibodies and colicin toxins. Secondly and more exciting we can now assemble denser free supported bilayers than ever before and this has enabled us to assemble asymmetric layers which more closely resemble the natural bacterial outer membrane system than ever before. This complex membrane system is now available for experiment and we shall observe the binding of the antibiotic protein colicin N to both systems.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24089955
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24089955
Provenance
Creator Professor Jeremy Lakey; Dr Chris Johnson; Ms Nat Arunmanee; Dr Stephen Holt; Dr Stella Valenzuela; Dr Alexandra Solovyova
Publisher ISIS Neutron and Muon Source
Publication Year 2015
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2012-12-10T09:05:46Z
Temporal Coverage End 2012-12-14T14:36:11Z