Dr Ivanhoe Leung

Biography

Ivan attained his undergraduate degree in Chemistry at the University of Oxford, as a member of St Peter’s College. He completed a DPhil in the laboratories of Profs Christopher J. Schofield FRS and Timothy D. W. Claridge, during which he applied NMR spectroscopy to study enzymes from an extended family of non-haem iron oxygenases that use 2-oxoglutarate as a cosubstrate. After his DPhil he spent a further  two  years in the same group as a postdoctoral research assistant, working on a variety of projects ranging from protein-ligand interactions, enzyme mechanisms, biocatalysis and enzyme inhibition. He has also spent time as a visitor in the laboratory of Dr Isabelle Landrieu at the Université Lille 1, during which he utilised biomolecular NMR techniques to study protein dynamics. Since September 2014, Ivan has been part of the University of Auckland. He is currently a Senior Lecturer in Chemical Biology.

For more information about Ivan and his research team, please visit his Research Group Website.

Research | Current

The research of the Leung Group lies broadly at the interface between chemistry and biology with a focus on protein strcuture, function, mechanism and their links to the proteins’ biological roles. Our research is multidisciplinary, including chemistry, enzymology, molecular biology and biophysical methods. We collaborate closely with a number of research groups from the Schools of Chemical and Biological Sciences, as well as colleagues from overseas including the UK and Germany. Some examples of our current research areas include:

Protein-ligand interactions

Protein-ligand interactions are fundamental to almost all biological processes in living organisms. These ligands range from small molecules to nucleic acids, peptides and proteins. We routinely apply biophysical techniques, including thermal shift assay, ITC, non-denaturing mass spectrometry and NMR spectroscopy, to screen for new protein ligands and quantify protein-ligand binding interactions. In addition, we also conduct method development work for the measurements of protein-ligand binding.

Example: Sci. Rep. 2017, 7, 43727.

Enzyme catalysis and inhibition

The understanding of enzyme catalysis and inhibition are critical to applications such as drug discovery and the development of agrochemicals. We apply biochemical and biophysical tools study enzyme kinetics and inhibition in order to understand the chemistry and mechanism of enzyme-catalysed reactions. We also apply protein NMR spectroscopy and X-ray crystallography to understand the structural bases of enzyme inhibitions.

Example: Bioorg. Med. Chem. Lett. 2017, 27, 277–281.

Posttranslational modification of proteins

Some proteins are known to undergo posttranslational modifications such as hydroxylation or phosphorylation. We apply biophysical and biochemical tools to visualise these modifications, and to study how posttranslational modification of proteins affect their structure, motion and function. 

Example: Org. Biomol. Chem. 2017, 15, 1100–1105.

Teaching | Current

● CHEM 100   Molecules that Changed the World

● CHEM 260   Introduction to Green Chemistry

● CHEM 350   Topics in Chemistry

● CHEM 360   Contemporary Green Chemistry

● CHEM 390   Medicinal Chemistry

● CHEM 738   Biomolecular Chemistry (Course Coordinator)

● CHEM 750   Advanced Topics in Chemistry

● PHARMACY 211   Applied Science for Pharmacy

● PHARMACY 213   Pharmacy 1 (Guest Lecturer)

Postgraduate supervision

For more detailed information about potential research projects please contact Ivan via email. The work offers the opportunity to learn about research at the interface between chemistry and biology, and receive training in molecular biology, enzymology and NMR spectroscopy.

Areas of expertise

● Biological and organic NMR spectroscopy

● Biophysical techniques in chemical biology

● Ligand screening and inhibitor discovery

● Mechanistic enzymology

● Protein chemistry

● Protein-directed dynamic combinatorial chemistry

● Protein-ligand interactions