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CD38 bound to hydrolysed cADPR analogue

Crystallography of a synthetic cADPR analogue bound to CD38 reveals more about the CD38 mechanism of ligand hydrolysis.

Joanna Watt

MChem, PhD, MRSC

Visiting Research Associate

  • Based at the University of Bath

My research uses synthetic chemistry to design molecules that will help us study calcium signalling in human cells.

Cell signalling forms part of vital processes, including cell division, fertilization and cell death. It is often dysfunctional in diseases like cancer, diabetes and inflammation. I hope that improving our understanding of these processes will also lead to new treatments for human disease.

I’m currently working on analogues of NAADP (Nicotinic Acid Adenine Dinucleotide Phosphate) – the most potent calcium releasing second messenger known to date. A combination of multiple negatively charged phosphate groups and the nicotinic acid make it both difficult to synthesize and challenging to study in biological systems. 

I’m also continuing projects on the other nucleotide second messengers, ADPR (Adenosine DiPhosphate Ribose) and cADPR (cyclic-ADPR) to study their role in calcium release and their formation by CD38.

Journal Covers

The first total synthesis of cIDPR depicted on the front cover of The Journal of Organic Chemistry - this stable, synthetic second messenger analogue releases calcium from intracellular stores.