Peptidomimetics as protein arginine deiminase 4 (PAD4) inhibitors was written by Trabocchi, Andrea;Pala, Nicolino;Krimmelbein, Ilga;Menchi, Gloria;Guarna, Antonio;Sechi, Mario;Dreker, Tobias;Scozzafava, Andrea;Supuran, Claudiu T.;Carta, Fabrizio. And the article was included in Journal of Enzyme Inhibition and Medicinal Chemistry in 2015.Category: piperazines This article mentions the following:
The protein arginine deiminase 4 (PAD4) is a calcium-dependent enzyme, which catalyzes 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-Jakob’s disease and cancer. In this study, the authors 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. In the experiment, the researchers used many compounds, for example, 1-(But-3-yn-1-yl)piperazine (cas: 911398-04-4Category: piperazines).
1-(But-3-yn-1-yl)piperazine (cas: 911398-04-4) belongs to piperazine derivatives. The piperazine scaffold is often found in biologically active compounds in different therapeutic areas. These therapeutic areas include antifungals, antidepressants, antivirals, and serotonin receptor (5-HT) antagonists/agonists. Piperazine and its salts did not induce point mutations in a bacterial test. A series of mutagenicity studies in cells, both in vitro and in vivo, has been completed and showed no evidence of mutagenic effect.Category: piperazines
Referemce:
Piperazine – Wikipedia,
Piperazines – an overview | ScienceDirect Topics