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Bioorg Med Chem. 2008 Sep 15;16(18):8349-58. doi: 10.1016/j.bmc.2008.08.046. Epub 2008 Aug 26.

CYP19 (aromatase): exploring the scaffold flexibility for novel selective inhibitors.

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  • 1Dipartimento di Scienze Farmaceutiche, Universit√† di Salerno, Via Ponte Don Melillo, I-84084 Fisciano (SA), Italy.


Several derivatives out of a series of antifungal agents exhibited a good inhibitory potency against aromatase as well as a fairly good selectivity toward CYP17, even if lacking H-bond accepting substituents. Their common structural feature is a flexible backbone that did not fit into previously reported CYP19 models. Thus, a ligand-based approach was exploited to develop a novel statistically robust, self-consistent and predictive 3D-QSAR model herein proposed as a helpful tool to design new aromatase inhibitors.

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