Publication: Molecular docking of aromatase inhibitors
Issued Date
2011-05-01
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ISSN
14203049
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2-s2.0-79957614697
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Mahidol University
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SCOPUS
Bibliographic Citation
Molecules. Vol.16, No.5 (2011), 3597-3617
Suggested Citation
Naravut Suvannang, Chanin Nantasenamat, Chartchalerm Isarankura-Na-Ayudhya, Virapong Prachayasittikul Molecular docking of aromatase inhibitors. Molecules. Vol.16, No.5 (2011), 3597-3617. doi:10.3390/molecules16053597 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/11716
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Title
Molecular docking of aromatase inhibitors
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Abstract
Aromatase is an enzyme that plays a critical role in the development of estrogen receptor positive breast cancer. As aromatase catalyzes the aromatization of androstenedione to estrone, a naturally occurring estrogen, it is a promising drug target for therapeutic management. The undesirable effects found in aromatase inhibitors (AIs) that are in clinical use necessitate the discovery of novel AIs with higher selectivity, less toxicity and improving potency. In this study, we elucidate the binding mode of all three generations of AI drugs to the crystal structure of aromatase by means of molecular docking. It was demonstrated that the docking protocol could reliably reproduce the interaction of aromatase with its substrate with an RMSD of 1.350 Å. The docking study revealed that polar (D309, T310, S478 and M374), aromatic (F134, F221 and W224) and non-polar (A306, A307, V370, L372 and L477) residues were important for interacting with the AIs. The insights gained from the study herein have great potential for the design of novel AIs. © 2011 by the authors.