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ISSN: 2167-0501

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Research Article

Synthesis and Evaluation of Ornithine Decarboxylase Inhibitors with Oxime Moiety and MCF-7 Breast Cancer Cells

Hyunshun Shin1*, Heather Whitehead2, Xian Zhou2, Karl L Banta3, Juliet V Spencer3, Myung K Cho4and Sung-Kun Kim4
1Department of Chemistry and Biochemistry, McMurry University, McM station Box 158, Abilene, TX 79697, USA
2Department of Chemistry, University of Iowa, Iowa City, IA 52242-1294, USA
3Department of Biology, University of San Francisco, 2130 Fulton Street, San Francisco, CA 94117, USA
4Department of Chemistry and Biochemistry, Baylor University, Waco, TX 76798-7348, USA
Corresponding Author : Hyunshun Shin
Department of Chemistry and Biochemistry
McMurry University, McM station Box 158
Abilene, TX 79697, USA
Tel: 325-793-3879
Fax: 325-793-4770
E-mail: [email protected], [email protected]
Received November 30, 2012; Accepted December 26, 2012; Published December 28, 2012
Citation: Shin H, Whitehead H, Zhou X, Banta KL, Spencer JV, Cho M, Kim SK. (2013) Synthesis and Evaluation of Ornithine Decarboxylase Inhibitors with Oxime Moiety and MCF-7 Breast Cancer Cells. Biochem Pharmacol 2:111. doi:10.4172/2167-0501.1000111
Copyright: © 2013 Shin H, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Cell proliferation can be regulated by small, aliphatic polyamines, and it is suggested that tumor tissues have significantly higher polyamine levels than surrounding tissues. The major biologically active polyamines present in mammalian cells are putrescine, spermidine, and spermine. The Ornithine Decarboxylase (ODC) catalyzes the decarboxylation of ornithine to produce putrescine which is precursor of polyamine synthesis. We report here the synthesis of 2-Amino-5-(Hydroxyimino) Pentanoic Acid (AHPA), based on the substrate of ODC, L-ornithine, derivatized with oxime functionality. In molecular docking studies, the E-isomer AHPA binds to ODC more favorably than does the
Z-isomer. In addition, the growth of MCF-7 (Michigan Cancer Foundation–7) breast cancer cells in the presence of AHPA was significantly reduced. These results implicate that AHPA a potentialt can be explored as a potential of cancer chemotherapy.

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