Dr Finian Leeper

University of Cambridge

University departments
Department of Chemistry

Position: Senior Lecturer
Personal home page: http://www.ch.cam.ac.uk/staff/fjl.html

PubMed journal articles - click here

Dr Finian Leeper is pleased to consider applications from prospective PhD students.

Research description

My interest lies in applying Organic Synthesis to Biological Problems. Current projects include (a) biosynthesis of prodigiosin - prodigiosin has potent antitumour and immunosuppressive properties and a close relative obatoclax is in clinical trials for multiple cancers. (b) synthesis of thiamin diphosphate (TPP) analogues for inhibition, mechanistic and crystallographic studies on TPP-dependent enzymes. Transketolase is a TPP-dependent enzyme that has been proposed as a target for anti-cancer drugs. (c) synthesis of analogues of porphobilinogen which would be inhibitors of tetrapyrrole biosynthesis. (d) new methods for the synthesis of radiotracers for PET imaging. Have also had a project on synthesis of contrast agents for MRI.

Research Programme or Virtual Institute
Advanced Cancer Imaging

Synthetic Chemistry Enzyme Assays

Recent publications:
 Retrieving latest data from feed...

Symplectic Elements feed provided by Research Information, University of Cambridge

Key publications

Erixon KM, Dabalos CL, Leeper FJ (2007), Inhibition of pyruvate decarboxylase from Z. mobilis by novel analogues of thiamine pyrophosphate: investigating pyrophosphate mimics, Chem. Commun.: 960-962. Williamson NR, Simonsen HT, Ahmed RAA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GPC (2005), Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces, Molec. Microbiology, 56(4): 971-989. Goodwin CE, Leeper FJ (2003), Stereochemistry and mechanism of the conversion of 5-aminolaevulinic acid into porphobilinogen catalysed by porphobilinogen synthase, Org. Biomolec. Chem., 1: 1443-1446.