Projects in my laboratory involve the development of both small molecules and peptidomimetics that interact with their biological target with high affinity.  As part of multi-disciplinary collaborations, we apply structural techniques, including nuclear magnetic resonance (NMR) spectroscopy and crystallography, to examine these molecular interactions at high resolution, and rationally alter ligand chemistry to produce compounds with desirable biochemical and pharmacological properties. Interaction kinetics are quantified using a variety of biophysical techniques such as fluorescence polarization and NMR spectroscopy, as well as surface plasmon resonance (SPR) using our state-of-the-art Biacore S200.

Peptidomimetic projects involve the rational design of peptide-based inhibitors of protein-protein interactions, using chemical modification to stabilise the peptides and improve their pharmacological potential.

Current projects include:

• Development of novel antibiotics targeting essential enzymes in Mycobacterium tuberculosis.
• Constrained peptidomimetics targeting PCNA – the human DNA sliding clamp – as a novel approach to cancer treatment.
• Constrained peptidomimetics as antagonists of nuclear receptor function, for applications in cancer, diabetes, and other diseases.