CYP19 (aromatase): exploring the scaffold flexibility for novel selective inhibitors.
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.
Castellano
Sabrina
S
Dipartimento di Scienze Farmaceutiche, Università di Salerno, Via Ponte Don Melillo, I-84084 Fisciano (SA), Italy.
Stefancich
Giorgio
G
Ragno
Rino
R
Schewe
Katarzyna
K
Santoriello
Marisabella
M
Caroli
Antonia
A
Hartmann
Rolf W
RW
Sbardella
Gianluca
G
D000935:Antifungal Agents / Q000138:chemical synthesis / Q000494:pharmacology*; D047072:Aromatase Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D015195:Drug Design; D008024:Ligands; D021281:Quantitative Structure-Activity Relationship; D013254:Steroid 17-alpha-Hydroxylase / Q000037:antagonists & inhibitors*
D000935:Antifungal Agents; D047072:Aromatase Inhibitors; D008024:Ligands; D013254:Steroid 17-alpha-Hydroxylase