PAD2 Activity Monitored via a Fluorescent Substrate Analog

Mary J. Sabulski, Yanming Wang, Marcos M. Pires

Research output: Contribution to journalArticlepeer-review


The post-transitional modification of peptidyl arginine to citrulline by PAD2 can affect the inherent biophysical properties of the citrullinated protein. Furthermore, dysregulation of PAD2 activity has been implicated in a number of human diseases. Inhibition of these enzymes by small molecules can serve as essential probes in establishing a link to pathogenesis. Herein, we describe a profluorescent substrate analog that reports on the activity and the inhibition of PAD2 in a robust assay. Most noteworthy, we expect future drug discovery efforts based on PAD2 inhibition can be pursued via this assay.

Original languageEnglish (US)
Pages (from-to)599-605
Number of pages7
JournalChemical Biology and Drug Design
Issue number4
StatePublished - Oct 1 2015

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry


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