Professor Alison Hulme FRSE
The Hulme group's research interests in natural products chemistry cover diverse fields, from synthetic organic chemistry and chemical biology, to historic textile dyestuffs. The group has a particular interest in the synthesis of natural products which interact with their biological targets through several, or many, chiral groups. The Hulme group has developed new stereocontrolled glycolate aldol reactions, and novel applications of the Evans-Tishchenko, Heck and ring-closing metathesis (RCM) reactions.
This methodology has allowed us to tackle the synthesis of a range of natural product targets including: iminosugars such as DAB-1; the protein synthesis inhibitor anisomycin; polyketides such as octalactin A; tetrahydroisoquinoline antibiotics such as pancratistatin; and products of mixed PKS-NRPS biosynthetic pathways, such as the C2-symmetric di-lactone, disorazole C1, and the unusual aminopolyol zwittermicin A.
At the Chemical Biology interface the Hulme group have pioneered the development of enabling synthetic methodology to allow the tagging and imaging of a range of biomolecules within the complex medium of a cell, or organism. The Hulme group has pioneered new approaches towards small-molecule target identification, and has developed a linker for affinity chromatography which is compatible with "click" chemistry, offering exciting new possibilities for target isolation. Their work on a RET-based sensor for copper(I), which is compatible with biological systems has been widely cited.
The Hulme group has also developed new synthetic methodology to selectively label the non-reducing end of glycosaminoglycans (GAGs) for the first time; and studies of protein-GAG interactions are being carried out with collaborators in Edinburgh and Manchester. The Hulme group also collaborates with the groups of Prof. Malcolm Walkinshaw (Institute of Structural and Molecular Biology, University of Edinburgh) and Profs. Ted Hupp and Kathryn Ball (Edinburgh Cancer Research Centre) on the design of interfacial inhibitors for the oncogenic protein MDM2.