Aromatase inhibition by the potent allosteric inhibitor AR13

Hormonal breast cancer therapies often modulate the activity of nuclear estrogen receptors, and aromatase.  Off-target binding, and drug resistance are challenges that curtail drug development.  After searching a broad compound library, we have evidence that our compound, AR13, binds at a distinct site from the native substrate.  Steps to provide kinetic, and structural evidence by protein crystallography will be discussed.  AR13 may bring rise to a novel class of aromatase inhibitors with diverse toxicity profiles.