A large variety of post-translational modifications can exist on the N-terminal tails of histone proteins H2A, H2B, H3 and H4. These have been of great interest as they have increasingly been shown to influence fundamental biological processes and human disease. Studying these modifications provides insight into their physiological functions and enables the search for potent small molecule inhibitors. In this thesis, new fluorescence-based supramolecular tools were developed and used to a) measure the binding of covalently modified peptide tails to a collection of synthetic receptors in neutral aqueous solution and b) monitor an enzyme that installs a post-translational modification (PTM) in real-time. Two different approaches were used to detect binding in these systems. The first was the optimization of a competitive dye-displacement method that relies on the ability of the cationic dye lucigenin. The second was the synthesis of novel conjugates that consist of calixarenes covalently appended with multiple different fluorescent dyes. / Graduate / 0487 / 0490 / 0491
| Identifer | oai:union.ndltd.org:uvic.ca/oai:dspace.library.uvic.ca:1828/5316 |
| Date | 29 April 2014 |
| Creators | Tabet, Sara |
| Contributors | Hof, Fraser Alan |
| Source Sets | University of Victoria |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Rights | Available to the World Wide Web |
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