Publication:
Molecular docking of aromatase inhibitors

dc.contributor.authorNaravut Suvannangen_US
dc.contributor.authorChanin Nantasenamaten_US
dc.contributor.authorChartchalerm Isarankura-Na-Ayudhyaen_US
dc.contributor.authorVirapong Prachayasittikulen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-05-03T08:07:29Z
dc.date.available2018-05-03T08:07:29Z
dc.date.issued2011-05-01en_US
dc.description.abstractAromatase 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.en_US
dc.identifier.citationMolecules. Vol.16, No.5 (2011), 3597-3617en_US
dc.identifier.doi10.3390/molecules16053597en_US
dc.identifier.issn14203049en_US
dc.identifier.other2-s2.0-79957614697en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/11716
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79957614697&origin=inwarden_US
dc.subjectChemistryen_US
dc.titleMolecular docking of aromatase inhibitorsen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=79957614697&origin=inwarden_US

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