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Journal of Biomolecular Screening
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1087057107301320v1
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Article

High-Throughput Mass Spectrometry Screening for Inhibitors of Phosphatidylserine Decarboxylase

Chris D. Forbes, Joshuaine G. Toth, Can C. Özbal, William A. LaMarr, Jennifer A. Pendleton, Sandra Rocks, Richard W. Gedrich, David G. Osterman, James A. Landro, Kevin J. Lumb*

Bayer Pharmaceuticals Corporation

* To whom correspondence should be addressed. E-mail: kevin_lumb{at}yahoo.com.


  Abstract
A high-throughput mass spectrometry assay to measure the catalytic activity of phosphatidylserine decarboxylase (PISD) is described. PISD converts phosphatidylserine to phosphatidylethanolamine during lipid synthesis. Traditional methods of measuring PISD activity are low throughput and unsuitable for the high-throughput screening of large compound libraries. The highthroughput mass spectrometry assay directly measures phosphatidylserine and phosphatidylethanolamine using the RapidFireTM platform at a rate of 1 sample every 7.5 s. The assay is robust, with an average Z'value of 0.79 from a screen of 9920 compounds. Of 60 compounds selected for confirmation, 54 are active in dose-response studies. The application of high-throughput mass spectrometry permitted a high-quality screen to be performed for an otherwise intractable target. (Journal of Biomolecular Screening XXXX:xx-xx)

First published on May 3, 2007, doi:10.1177/1087057107301320

Journal of Biomolecular Screening 2007;12:628.

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

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Home page
 J Biomol ScreenHome page
R. Rathore, J. Corr, G. Scott, P. Vollmerhaus, and K. D. Greis
Development of an Inhibitor Screening Platform via Mass Spectrometry
J Biomol Screen, December 1, 2008; 13(10): 1007 - 1013.
[Abstract] [PDF]