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2011•Chemical CommunicationsOpen access

Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibition

Sara Maurelli, Mario Chiesa, Elio Giamello, Giovanna Di Nardo, Valentina Elisabetta Viviana Ferrero, Gianfranco Gilardi, Sabine Van Doorslaer

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Abstract

Aromatase (CYP19A1), is a microsomal cytochrome P450 catalysing the conversion of androgens to estrogens. Non-steroidal inhibitors, such as anastrozole, are important drugs in breast cancer therapy. Using hyperfine sublevel correlation (HYSCORE) spectroscopy we provide the first experimental evidence of the binding of anastrozole to the iron heme of human aromatase.

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What this paper is about

Aromatase (CYP19A1), is a microsomal cytochrome P450 catalysing the conversion of androgens to estrogens. Non-steroidal inhibitors, such as anastrozole, are important drugs in breast cancer therapy. Using hyperfine sublevel correlation (HYSCORE) spectroscopy we provide the first experimental evidence of the binding of anastrozole to the iron heme of human aromatase.

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Available abstract

Aromatase (CYP19A1), is a microsomal cytochrome P450 catalysing the conversion of androgens to estrogens. Non-steroidal inhibitors, such as anastrozole, are important drugs in breast cancer therapy. Using hyperfine sublevel correlation (HYSCORE) spectroscopy we provide the first experimental evidence of the binding of anastrozole to the iron heme of human aromatase.

Key concepts: Aromatase, Anastrozole, Microsome, Heme, Cytochrome P450, Chemistry, Aromatase inhibitor, Cancer research

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