Our research focuses on controlling protein-protein and protein-DNA interactions.

Work in the research group focuses on targeting biomolecular interactions in cancer highlighted by mutations in non-cancerous disease. We have expertise in the design of protein-protein interaction modulators and their evaluation in in vitro protein assays and cellular assays. We use peptides derived from the natural protein partners as scaffolds to identify small molecule inhibitors, suitable for drug development.

Current projects look at 1) inhibiting the immune checkpoint of PD-1/PD-L1 by developing small molecules based on cyclic peptides. 2) Inhibiting the protein-protein interactions in telomerase based on mutations observed in early ageing diseases. 3) Inhibiting the protein-protein interactions of the transcription factors Nrf2 and MafG based on mutations observed in inflammation related cataracts. 4) Controlling protein-protein interactions in the cell division machinery of actinobacteria to identify new antibiotic targets with greater specificity.

A key element of our research includes the application of new methods to design drug like small molecules capable of controlling biomolecular interactions. Our method, peptide-directed binding, uses bioactive peptides as scaffolds to identify small molecular peptide mimetics able to control the target interaction. Peptide-directed binding has remarkably high hit rates with few compounds prepared, enabling the identification of chemical probes and leads.