Profiling Protein Arginine Deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors
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Publisher version
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2008-01-15Keywords
Arthritis, RheumatoidChlortetracycline
Combinatorial Chemistry Techniques
Enzyme Inhibitors
Fluorescent Dyes
Hydrolases
Minocycline
Models, Biological
Molecular Structure
StreptomycinTetracyclineProtein Arginine Deiminase 4MinocyclineStreptomycinChlortetracyclineTetracyclineRheumatoid ArthritisDMARDarginineAssayScreenArginine deiminaseInhibitorRhodamineF-amidineFluoroRFAActivity-Based Protein ProfilingABPPBiochemistryEnzymes and CoenzymesMedicinal-Pharmaceutical ChemistryTherapeutics
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Protein Arginine Deiminase 4 (PAD4) has emerged as a leading target for the development of a Rheumatoid Arthritis (RA) pharmaceutical. Herein, we describe the development of a novel screen for PAD4 inhibitors that is based on a PAD4-targeted Activity-Based Protein Profiling reagent, denoted Rhodamine-conjugated F-Amidine (RFA). This screen was validated by screening 10 Disease Modifying Anti-Rheumatic Drugs (DMARDs) and identified streptomycin, minocycline, and chlortetracycline as micromolar inhibitors of PAD4 activity.Source
Bioorg Med Chem. 2008 Jan 15;16(2):739-45. Link to article on publisher's site. Epub 2007 Oct 13.DOI
10.1016/j.bmc.2007.10.021Permanent Link to this Item
http://hdl.handle.net/20.500.14038/50065Notes
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.