Chloroacetamidine-Based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and In Vitro and In Vivo Evaluation

• Published in: Chembiochem : a European journal of chemical biology Vol. 11; no. 9; pp. 1219 - 1223
• Main Authors: Obianyo, Obiamaka, Causey, Corey P, Osborne, Tanesha C, Jones, Justin E, Lee, Young-Ho, Stallcup, Michael R, Thompson, Paul R
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 14.06.2010; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: Amidines - chemical synthesis; Amidines - chemistry; Amidines - pharmacology; Arginine - metabolism; Catalytic Domain; Cell Line; Cl-amidine; Enzyme Inhibitors - chemical synthesis; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - pharmacology; enzymes; Humans; inhibitors; Methylation; Peptides - chemical synthesis; Peptides - chemistry; Peptides - pharmacology; protein arginine methyltransferase; Protein-Arginine N-Methyltransferases - antagonists & inhibitors; Protein-Arginine N-Methyltransferases - metabolism; transcription
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201000209

Protein arginine methyltransferases (PRMTs) catalyze the post‐translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.