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Journal of Biomolecular Screening
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Article

High-Throughput Identification of Inhibitors of Human Mitochondrial Peptide Deformylase

Christophe Antczak, David Shum, Sindy Escobar, Bhramdeo Bassit, Earl Kim, Venkatraman E. Seshan, Nian Wu, Guangli Yang, Ouathek Ouerfelli, Yue-Ming Li, David A. Scheinberg, Hakim Djaballah*

* To whom correspondence should be addressed. E-mail: djaballh{at}mskcc.org.


  Abstract
The human mitochondrial peptide deformylase (HsPDF) provides a potential new target for broadly acting antiproliferative agents. To identify novel nonpeptidomimetic and nonhydroxamic acid-based inhibitors of HsPDF, the authors have developed a high-throughput screening (HTS) strategy using a fluorescence polarization (FP)-based binding assay as the primary assay for screening chemical libraries, followed by an enzymatic-based assay to confirm hits, prior to characterization of their antiproliferative activity against established tumor cell lines. The authors present the results and performance of the established strategy tested in a pilot screen of 2880 compounds and the identification of the 1st inhibitors. Two common scaffolds were identified within the hits. Furthermore, cytotoxicity studies revealed that most of the confirmed hits have antiproliferative activity. These findings demonstrate that the designed strategy can identify novel functional inhibitors and provide a powerful alternative to the use of functional assays in HTS and support the hypothesis that HsPDF inhibitors may constitute a new class of antiproliferative agent. (Journal of Biomolecular ScreeningXXXX:xx-xx)

First published on April 13, 2007, doi:10.1177/1087057107300463

Journal of Biomolecular Screening 2007;12:521.

A more recent version of this article appeared on June 1, 2007

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