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Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer

Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer

Tarun Jha, Nilanajn Adhikari, Amit Kumar Halder, Achintya Saha
Copyright: © 2017 |Pages: 69
ISBN13: 9781522505495|ISBN10: 1522505490|EISBN13: 9781522506386
DOI: 10.4018/978-1-5225-0549-5.ch004
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MLA

Jha, Tarun, et al. "Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer." Oncology: Breakthroughs in Research and Practice, edited by Information Resources Management Association, IGI Global, 2017, pp. 118-186. https://doi.org/10.4018/978-1-5225-0549-5.ch004

APA

Jha, T., Adhikari, N., Halder, A. K., & Saha, A. (2017). Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer. In I. Management Association (Ed.), Oncology: Breakthroughs in Research and Practice (pp. 118-186). IGI Global. https://doi.org/10.4018/978-1-5225-0549-5.ch004

Chicago

Jha, Tarun, et al. "Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer." In Oncology: Breakthroughs in Research and Practice, edited by Information Resources Management Association, 118-186. Hershey, PA: IGI Global, 2017. https://doi.org/10.4018/978-1-5225-0549-5.ch004

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Abstract

Aromatase is a multienzyme complex overexpressed in breast cancer and responsible for estrogen production. It is the potential target for designing anti-breast cancer drugs. Ligand and Structure-Based Drug Designing approaches (LBDD and SBDD) are involved in development of active and more specific Nonsteroidal Aromatase Inhibitors (NSAIs). Different LBDD and SBDD approaches are presented here to understand their utility in designing novel NSAIs. It is observed that molecules should possess a five or six membered heterocyclic nitrogen containing ring to coordinate with heme portion of aromatase for inhibition. Moreover, one or two hydrogen bond acceptor features, hydrophobicity, and steric factors may play crucial roles for anti-aromatase activity. Electrostatic, van der Waals, and p-p interactions are other important factors that determine binding affinity of inhibitors. HQSAR, LDA-QSAR, GQSAR, CoMFA, and CoMSIA approaches, pharmacophore mapping followed by virtual screening, docking, and dynamic simulation may be effective approaches for designing new potent anti-aromatase molecules.

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