Title

A fluopol-ABPP HTS assay to identify PAD inhibitors

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

10-14-2010

Document Type

Article

Subjects

Arthritis, Rheumatoid; Cell Line, Tumor; Drug Evaluation, Preclinical; Enzyme Inhibitors; Fluorescence Polarization; Fluorescent Dyes; High-Throughput Screening Assays; Humans; Hydrolases; Inhibitory Concentration 50; Streptonigrin

Disciplines

Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics

Abstract

Protein Arginine Deiminase (PAD) activity is dysregulated in numerous diseases, e.g., Rheumatoid Arthritis. Herein we describe the development of a fluorescence polarization-Activity Based Protein Profiling (fluopol-ABPP) based high throughput screening assay that can be used to identify PAD-selective inhibitors. Using this assay, streptonigrin was identified as a potent, selective, and irreversible PAD4 inactivator.

DOI of Published Version

10.1039/c0cc02634d

Source

Chem Commun (Camb). 2010 Oct 14;46(38):7175-7. doi: 10.1039/c0cc02634d. Link to article on publisher's site. Epub 2010 Aug 25.

Journal/Book/Conference Title

Chemical communications (Cambridge, England)

Comments

At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed