Protein Structure, Mechanism and Design

Proteins are large biomolecules made up of chains of amino acids that perform a diverse array of functions within living organisms. Enzymes are a class of protein that catalyse reactions.

Histone deacetylase (HDAC) enzymes are key enzymes involved in a number of diseases such as cancer and Alzheimer's disease.

Researchers at Leicester are using novel peptide probe molecules to understand how this process works in order to develop novel drugs that are highly potent and have fewer side effects than the drugs that are currently available.

Understanding the mechanisms of a number of redox enzymes such as cytochrome P450 is an important area of research at Leicester. Recent work in this area has focused on understanding substrate specificity in the heme peroxidases.

Amphotericin B is a molecule produced by the soil bacterium Streptomyces nodosus and, despite considerable toxicity, it has been a leading broad-spectrum antifungal antibiotic for more than fifty years. Leicester researchers are using protein-engineering techniques to develop analogues of amphotericin that are potent, but non-toxic.

Sample Research Articles

Peptide Scanning for Studying Structure-Activity Relationships in Drug Discovery. A.G. Jamieson, N. Boutard, D. Sabatino, W.D. Lubell, Chem. Biol. Drug Des., 2013, 81, 148-165.

Redesign of polyene macrolide glycosylation: Engineered biosynthesis of 19-(O)-perosaminyl-amphoteronolide B. E. Hutchinson, B. Murphy, T. Dunn, C. Breen. B. Rawlings and P. Caffrey, Chem. Biol., 2010, 17, 174-182.

An analysis of substrate binding interactions in the heme peroxidase enzymes: a structural perspective A. Gumiero, E.J. Murphy, C.L. Metcalfe, P.C.E Moody, E.L. Raven, Arch. Biochem. Biophys. 2010, 500, 13-20.

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Department of Chemistry
University of Leicester
Leicester, LE1 7RH, UK


Tel: [+44] (0)116 252 2100

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