Alan Stewart Group – Metal ions in Medicine

Group Highlights

Our work is centred on how metal ions, such as Zn2+, Ca2+ and Co2+ are transported through the blood and how their mishandling can lead to disease. A key part of my group’s activity is the study of their interactions with circulatory proteins. At a cell and systems level, we are interested in how these interactions have a functional impact. We commonly utilise methods that examine the movement of Zn2+ and Ca2+ ions within cells and across membranes or measure their direct physiological functional outputs (e.g. coagulatory processes). Over the last few years, we have also worked closely with colleagues across the North Haugh particularly, the Mass Spectrometry Facility in St Andrews in the utilisation of quantitative proteomics clinical studies.

Please visit our group website: https://metalion.wp.st-andrews.ac.uk/

Effects of fatty acid binding at the FA2 site on the primary zinc site of human serum albumin. (A) Structure of HSA with 5 molecules of myristate bound (PDB: 1BJ5). (B) Overlay of the main zinc-binding site in the myristate-bound structure (in green; PDB: 1BJ5) and the zinc-bound structure (in blue; PDB: 5IJF). A structural change is induced by fatty acid binding. This triggers the zinc-coordinating residue His67 to move 8 Å away from the other two coordinating side chains. Figure taken from Sobczak et al. (2021) Chem. Sci. 12: 4079-4093.