Inhibitors of the enzyme aromatase are of significant medicinal value since the enzyme is a target for drugs against hormone-dependent breast cancer.  Isoflavanones are a class of natural compounds that has shown good potency against aromatase. We determined the inhibitory potencies of about 20 synthesized isoflavanones using a fluorescence-based bioassay with human aromatase. In order to explore the intermolecular interactions responsible for inhibitor binding and to guide future synthetic efforts, we computationally docked the structures of active isoflavanones into the X-ray crystal structure of aromatase. Analysis of the docking results identified hydrophobic interactions along with arene-arene interactions as the main driving forces for inhibitor binding.

Evaluation of isoflavanones as aromatase inhibitors by experimental and computational methods

243rd National Meeting (2012)

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