
Encourages creativity and critical thinking.
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Helen Hailes is Professor of Chemical Biology in the Department of Chemistry at University College London. She obtained her PhD in organic chemistry from the University of Cambridge in 1991 under the supervision of Professor Jim Staunton. She then carried out postdoctoral research at the University of Cambridge and at Imperial College London with Professor Steve Ley and Dr David Widdowson. In 1994, Hailes joined the Department of Chemistry at University College London as a Lecturer, becoming Senior Lecturer in 2002, Reader in 2005, and Professor of Chemical Biology in 2010.
Her research group develops sustainable strategies for molecular assembly using biocatalysts, focusing on single-step reactions, multi-step cascades, and processes in water. Projects include biocatalyst discovery through functional metagenomics and the use of enzymes such as transaminases, transketolases, ene reductases, decarboxylases, tyrosinases, imine reductases, alcohol dehydrogenases, methyltransferases, and norcoclaurine synthases. Additional efforts involve transforming biomass waste into higher-value compounds and employing enzymes for the degradation of plastics and other waste materials to enable molecular recycling. The group also applies organic chemistry to biological problems, including the synthesis of lipid conjugates for nanoparticle delivery and imaging agents, investigations into the photoactive behaviour of GFP, and the development of chemotherapeutics as anti-tuberculosis, anti-viral, and anti-bacterial agents. These activities have resulted in prizes from the Royal Society of Chemistry and the Institution of Chemical Engineers. Hailes has published over 270 papers, garnering more than 7,000 citations. Key publications include 'Enzymatic synthesis of benzylisoquinoline alkaloids using norcoclaurine synthase' (Nature Communications, 2022), 'Mechanoenzymatic reactions for the hydrolysis of PET' (Nature Communications, 2023), and 'The use of tyrosinases in a chemoenzymatic cascade as a peptide ligation strategy' (RSC Chemical Biology, 2023).
