Parkinson, Claire Louise (2010) Functionalised PDA liposomes as biosensors for proteins. PhD thesis, University of Glasgow.Due to Embargo and/or Third Party Copyright restrictions, this thesis is not available in this service.
A synthetic membrane is an organized supramolecular membrane that encompasses molecular recognition with signal transduction analogous to a natural biosensing system in a cell membrane. These synthetic based models allow the study and application of receptor-ligand binding to biosensor design. In order to enable a recognition event and a response the liposome incorporates a known ligand with a suitable receptor interaction that upon complementary binding can elicit a measurable response. Polydiacetylene based sensors have been previously considered and utilised for the detection of biologically important species due to the stimuli-responsive colour changing properties. These colorimetric biosensors are self-assemblies of diacetylene lipids mixed with natural or synthetic biological receptor molecules. Polydiacetylene liposomes functionalised with molecular recognition groups can bind and thus detect colorimetrically if the binding is complementary. Biodetection of an analyte in aqueous media requires that the structure of the diacetylenic compound is able to form a stable dispersion in water, polymerizes efficiently yielding a coloured material, incorporating a suitable receptor that binds with an analyte and transduction of the binding interaction by means of a colour change. The structural features to be considered are chain length, solubility, amphiphilicity, functional group for modification.
|Item Type:||Thesis (PhD)|
|Subjects:||Q Science > QD Chemistry|
|Colleges/Schools:||College of Science and Engineering > School of Chemistry|
|Supervisor's Name:||Cooke, Dr. Graeme|
|Date of Award:||2010|
|Embargo Date:||14 May 2016|
|Depositing User:||Mrs Marie Cairney|
|Copyright:||Copyright of this thesis is held by the author.|
|Date Deposited:||14 Apr 2011|
|Last Modified:||15 Apr 2014 15:31|
Actions (login required)