Premium
PAD2 Activity Monitored via a Fluorescent Substrate Analog
Author(s) -
Sabulski Mary J.,
Wang Yanming,
Pires Marcos M.
Publication year - 2015
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12526
Subject(s) - small molecule , chemistry , citrulline , substrate (aquarium) , biophysics , drug discovery , arginine , biochemistry , microbiology and biotechnology , pharmacology , biology , amino acid , ecology
The post‐transitional modification of peptidyl arginine to citrulline by PAD 2 can affect the inherent biophysical properties of the citrullinated protein. Furthermore, dysregulation of PAD 2 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 PAD 2 in a robust assay. Most noteworthy, we expect future drug discovery efforts based on PAD 2 inhibition can be pursued via this assay.