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Amy O'Reilly


October 2012 - Present PhD Biochemistry/Biophysics.

2011 - 2012 MSc Mathematical Biology and Biophysical Chemistry, The University of Warwick

June 2011 - October 2011: BBSRC Research Council, Polaris House, Swindon.

2007 - 2010 BSc Biological Sciences with Cell Biology: 2.1. University of Warwick

Publications:

Rodolis, M., Mihalyi, A., O'Reilly, A., Slikas, J., Roper, D., Hancock, R., Bugg, TDH. Identification of a Novel Inhibition Site in Translocase MraY Based upon the Site of Interaction with Lysis Protein E from Bacteriophage PhiX174 (2014) ChemBioChem (PDF Document).pdf

Galley, NG., O'Reilly, AM., Roper, DI., Prospects for Novel Inihibitors of Peptidoglycan Transglycosylases (2014) BioOrganicChemistry (PDF Document).pdf

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PhD title:

Exploration and Analysis of Penicillin Binding Proteins as synthetic tools and targets. Investigating the Structure and Functional of Penicillin-Binding Proteins (PBPs) in Gram negative bacteria.

Peptidoglycan is a structurally vital component of the bacterial cell wall and its biosynthesis is heavily targeted by antibacterial therapeutics. Resistance mechanisms have evolved naturally in bacteria to evade destruction by antibiotics, which has recently assisted the emergence of nosoco

mial infections such as MRSA and VRE. This project aims to further investigate the structure and function of Penicillin-Binding Proteins (PBPs) in Gram-negative bacteria, with a focus to develop an assay for the full characterisation of the dual-activity of bifunctional PBPs. The mesh-like structure of peptidoglycan within the

cell wall consists of aligned glycan strands, which are cross-linked to each other via a peptide bridge. PBPs have a role in the building and cross-linking of these glycan strands. Synthesis of the glycan strand is to be tracked in real-time by Linear Dichroism. PBP activity is to be enzymatically characterised using biochemical and biophysical techniques, radio- and fluorescence-labelling and lipid-linked reagent chemistry. Advances in chemi

cal probe and substrate design at Warwick will aid this project, with chemical synthesis being used to harvest compounds required for assays. Mutants will be made by traditional molecular biology techniques to further elucidate the precise role of

individual PBP domains. A detailed understanding of peptidoglycan synthesis is of immediate interest to the pharmaceutical industry, since it will enable the design and application of novel assays to detect inhibitors of peptidoglycan polymerisation.

Conferences Attended:

1. MOAC DTC Annual Conference 28th - 30th July 2014, Stratford Upon Avon, UK.

2. Chemical Biology Conference, 1st - 2nd May 2014, Imperial College London, UK

3. Antibiotic Resistance Mechanisms Workshop for Researchers 28th - 29th November 2013, Birmingham, UK.

4. The Great Wall Symposium, 23rd - 25th September 2013, Institut Pasteur, Paris.

5. Chemical Biology Conference, 13th - 14th June 2013, Imperial College London, UK

6. MOAC DTC Annual Conference, 28th - 31st May 2013, Ironbridge, UK.

7. Membrane Protein Crystallisation, 27th September 2012, Diamond Light Source, Oxford, UK.

8. CCP4 Protein Structure and Function Conference, 5th - 7th september 2012, Carlisle, UK.

9. MOAC DTC Annual Conference 24th- 27th July 2012, Buxton, UK.


End of MSc

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