title: A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1.
abstract: The dysregulation of protein arginine methyltransferases (PRMTs) is implicated in a wide variety of disease states. Here we report the design, synthesis, and screening of a combinatorial peptide library used to characterize the substrate specificity of PRMT1. The information gained from this approach was used to develop a PRMT1 inhibitor with enhanced selectivity.
authors.affiliation: Department of Chemistry and Biochemistry, University of South Carolina, 631 Sumter St, Columbia, South Carolina, USA.
authors.forename: Kevin L
authors.initials: KL
authors.lastname: Bicker
authors.forename: Obiamaka
authors.initials: O
authors.lastname: Obianyo
authors.forename: Heather L
authors.initials: HL
authors.lastname: Rust
authors.forename: Paul R
authors.initials: PR
authors.lastname: Thompson
mesh_terms: D000595:Amino Acid Sequence; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D008969:Molecular Sequence Data; D019151:Peptide Library; D011484:Protein-Arginine N-Methyltransferases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D019151:Peptide Library; D011484:Protein-Arginine N-Methyltransferases