Abstract
Using molecular modelling techniques, information regarding the active site of oestrone sulphatase was determined. The structural properties of non-steroidal inhibitors required for inhibitory activity against oestrone sulphatase were investigated, and we were able to rationalize the inhibitory activity of both steroidal and non-steroidal inhibitors. The C(17) polar group within the structure of the substrate, oestrone sulphate, was required for potent inhibitory activity. The major requirement of inhibitors appeared to be the mimicking of the steroid C(3) sulphonate group. The phenolic ring in the oestrogen-based inhibitors (and the majority of the non-steroidal inhibitors) was not necessary for inhibitory activity. We synthesized a number of potential non-steroidal straight-chain alcohol-derived inhibitors for biochemical evaluation.
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