Research

Research in my group focuses on understanding how nutrient transporters function at a molecular level. In humans, many of the membrane proteins involved in absorbing nutrients from our diet are also responsible for drug transport and distribution into specific organs, including the central nervous system, liver, kidneys and GI tract. Nutrient transporters therefore have a profound impact on the pharmacokinetic properties of many administered drugs with clear medical advantages in understanding their structure, biochemistry and regulation.

Transporters belonging to the Solute Carrier (SLC) family are integral membrane proteins that play essential roles in human physiology. They predominantly function to regulate the transport of small molecules into and out of cells. However, SLC families have been linked to intracellular signalling networks, particularly with respect to amino acid and nutrient sensing. We are interested in understanding the molecular basis for ligand recognition in the SLC transporters, how they couple transport to secondary ion gradients, their roles in drug transport and the mechanisms used to regulate their function in the cell.

The group is currently working on several families of proton coupled SLC transporters linked to drug uptake and retention in the human body. These include the SLC15 peptide transporters, PepT1 and PepT2, the SLC7, 36 and 38 families of amino acid transporters and the SLC35 family of nucleotide sugar transporters.

We are a structural and biochemistry focused group, using a range of biophysical and biochemical methods. Our main techniques are protein crystallisation and single particle cryo-EM imaging. We also rely heavily on insights gained through detailed biochemical analysis of reconstituted protein and functional assays. Our research has resulted in several commercial products in the area of membrane protein structural biology. Please see the individual pages for specific projects, research papers, review articles and book chapters; I hope you enjoy the site.