Phillip J. Stansfeld

The Stansfeld group studies one of the fundamental challenges in biological sciences: to visualise biomolecular machines in high-resolution detail. This is notoriously difficult, expensive and time-consuming to achieve by using experimental techniques, especially for proteins that exist in cell membranes, known as Integral membrane proteins. These proteins play fundamental roles in cell biology e.g. as processing enzymes, ion channels, drug receptors, and solute transporters. With the increasing threat of antimicrobial resistance, we are especially interested in bacterial membrane proteins. Knowledge of the three-dimensional structures of proteins involved in essential processes provides the physical details of potentially viable targets for killing drug-resistant, pathogenic bacteria. By animating these structures in computers, we may assess the association of proteins with lipids, drug molecules and other essential components of the protein complexes.

Murphy, Roisin, Fairbairn, Julia A., Baileeves, Becca W. A., Stansfeld, Phillip J. and Bugg, Timothy D. H. (2026) 4-Aryl-2-aminoimidazole analogues of bromoageliferin with antimicrobial activity against Acinetobacter baumannii show in vitro inhibition of translocase MraY on the peptidoglycan biosynthesis pathway. Bioorganic & Medicinal Chemistry Letters, 136 . 130597. doi:10.1016/j.bmcl.2026.130597 ISSN 0960-894X. McAndrew, Martin B. L., Cook, Jonathan P., Gill, Amy, Sahoo, Kavya, Thomas, Clare, Stansfeld, Phillip J. and Crow, Allister (2025) Structural characterization of the YbbAP-TesA ABC transporter identifies it as a lipid hydrolase complex that extracts hydrophobic compounds from the bacterial inner membrane. PLoS Biology, 23 (11). e3003427. doi:10.1371/journal.pbio.3003427 ISSN 1545