The Armstrong Group uses chemical biology techniques to study glycan editing enzymes.

Human cells are coated with a dense array of carbohydrates that are attached to proteins and lipids — together termed the glycocalyx. The majority of soluble secreted proteins are also similarly decorated with glycans. The glycocalyx mediates – among other things – cell to cell adhesion, signalling, immune cell maturation and pathogen invasion. The various glycan structures present in the glycocalyx can be modified with both acetyl and sulfate groups. Although these carbohydrate modifications may seem subtle, they can have a profound impact on human health. My research program will rely on the development of new chemical tools to study carbohydrate editing in-vivo. These chemical tools will also enable the development of new therapeutics that target both host and pathogen carbohydrate modifying enzymes.

Our lab uses a variety of chemical biology techniques to solve real-world problems. We use organic chemical synthesis to create new inhibitors and probes for human and pathogen enzymes. The structural biology methods of X-ray crystallography and Single-Particle Electron-Cryomicroscopy (Cryo-EM) allow us to identify the binding sites and modes of synthetic probes and inhibitors. Activity-Based Protein Profiling (ABPP) allows us to gain new knowledge across multiple scales using our synthetic probes.