Biotransformation and molecular docking studies of aromatase inhibitors

Glenroy Martin*, Javier Narvaez, Rachel Bulmer, Marcus Durrant

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
8 Downloads (Pure)


Bioconversion of the aromatase inhibitor formestane (4-hydroxyandrost-4-ene-3,17-dione) by the fungus Rhizopus oryzae ATCC 11145 resulted in a new minor metabolite 3,5α-dihydroxyandrost-2-ene-4,17-dione and the known 4β,5α-dihydroxyandrostane-4,17-dione as the major product. The structural elucidation and bioactivities of these metabolites are reported herein. Molecular modeling studies of the interactions between these metabolites and the aromatase protein indicated that acidic (D309), basic (R115), polar (T310), aromatic (F134, F221, and W224), and non-polar (I133, I305, A306, V369, V370, L372, V373, M374, and L477) amino acid residues contribute important interactions with the steroidal substrates. These combined experimental and theoretical studies provide fresh insights for the further development of more potent aromatase inhibitors.
Original languageEnglish
Pages (from-to)95-102
Early online date12 Jul 2016
Publication statusPublished - 1 Sept 2016


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