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The thioredoxin redox system, consisting of the thioredoxin protein, thioredoxin reductase and NADPH, is ubiquitous in all living cells and is known to be important in a multitude of biological functions, including cell cycle regulation and maintaining an intracellular reduced state [1]. Studies in various human malignancies and cell lines in vitro have shown an up regulation of thioredoxin and have demonstrated a definite link between thioredoxin and cancer [2], [3]. Thioredoxin levels have also been shown to be raised in the presence of superoxide generating drugs, thus suggesting that inhibition of this redox system may also lead to improved efficiency of these drugs. The crystallisation of a variety of thioredoxin proteins has allowed comparisons to be made between crystal structures of mammalian and bacterial thioredoxins. Studies of existing human thioredoxin complexes have also enabled the understanding of the specificity requirements that thioredoxin has for its target proteins [4]. This has facilitated the design of potential novel inhibitors of the active site of this redox protein. There are currently two novel heteroaromatic quinol inhibitors, which have shown to have activity against thioredoxin, under development at the Cancer Research Laboratories of the University of Nottingham. These inhibitors are thought to have a novel mode of action, each containing a bis-micheal acceptor, allowing them to irreversibly bind to the active site, thus irreparably inactivating the protein. By studying the crystal structure of thioredoxin-inhibitor complex it will be possible to apply structure-activity relationships and thus enable not only the understanding of how these heteroaromatic quinols block the activity of thioredoxin, but also to develop these drugs with the intention of improving their affinity for the binding site. N labelled NMR HSQC experiments have also provided an insite into the binding of these quinols to the thioredoxin active site and thereby facilitating further drug design to improve affinity.

Simulation of the absorption of acetone on ice at surfaces, bulk ice and small-angle grain boundaries