The Chemistry/Biology Interface

The Chemistry/Biology Interface area is broad, with particular strengths in the areas of protein structure and function, mechanistic enzymology, proteomics, biologically targeted synthesis, the application of high throughput and combinatorial approaches and biophysical chemistry, which focuses on the development and application of physicochemical techniques to biological systems.
Research within this theme encompasses the study of protein structure and function, mechanistic enzymology, proteomics, biocatalysis and biotransformations, the application of biophysical techniques to complex biological systems, and the application of chemical tools, including high-throughput approaches, to answer and address important biomedical questions and needs. Key strengths include (i) Structural and molecular biology (Barlow, Bode, Botting, Daff, Dryden, Lovett, Mitchell, Mowat, Naismith, Uhrin) focused on understanding how proteins control their function in problems ranging from cancer to microbial infection, (ii) Total synthesis, and the application of biologically active molecules and materials (Bradley, CCampbell, Campopiano, Florence, Goss, Hulme, Lawrence, Lilienkampf, Mount, Nudelman, O'Hagan, Smith, Westwood), (iii) The application of the tools of chemistry to control stem cell fate and cellular regeneration, and in the area of optical and electrochemical molecular sensing and imaging (Bradley, CCampbell, Lilienkampf, Mount, Vendrell).
The research activities include three complementary and multidisciplinary research consortia: the Biomedical Sciences Research Complex (BSRC, director: Naismith); the Centre for Translational and Chemical Biology (CTCB, co-director Barlow) and the Interdisciplinary Research Collaboration (IRC) in Molecular Sensing and Imaging (PI: Bradley), conceived to enhance synergistic interactions between chemistry, biology, medicine, engineering, and physics.

Research Highlights since 2008

Selected highlights include a new model of an ion channel gating mechanism (Naismith, Science 2008), palladium-mediated intracellular chemistry (Bradley, Nature Chem 2011) and protein-directed dynamic chemistry (Campopiano, Nature Chem 2010). Naismith determined the structure of a RING E3 ligase bound to ubiquitin-loaded E2 (Nature 2012). Barlow and Uhrin determined the structure of complement factor H (CCPs 19-20) bound to C3d (Nature Struct. Bio 2011).