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Updated: Apr 24, 2026

Fluorescence-based Monitoring of PAD4 Activity via a Pro-fluorescence Substrate Analog
Published on: November 5, 2014
Peptidomimetics as protein arginine deiminase 4 (PAD4) inhibitors
Andrea Trabocchi1, Nicolino Pala, Ilga Krimmelbein
1Department of Chemistry "Ugo Schiff", University of Florence , Sesto Fiorentino, Florence , Italy .
Abstract:
The protein arginine deiminase 4 (PAD4) is a calcium-dependent enzyme, which catalyses the irreversible conversion of peptidyl-arginines into peptidyl-citrullines and plays an important role in several diseases such as in the rheumatoid arthritis, multiple sclerosis, Alzheimer's disease, Creutzfeldt-Jacob's disease and cancer. In this study, we report the inhibition profiles and computational docking toward the PAD4 enzyme of a series of 1,2,3-triazole peptidomimetic-based derivatives incorporating the β-phenylalanine and guanidine scaffolds. Several effective, low micromolar PAD4 inhibitors are reported in this study.
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