A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology



Document Type


Medical Subject Headings

Amino Acid Sequence; Enzyme Inhibitors; Humans; Molecular Sequence Data; Peptide Library; Protein-Arginine N-Methyltransferases; Substrate Specificity


Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics


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.

Rights and Permissions

Citation: Mol Biosyst. 2011 Jan;7(1):48-51. doi: 10.1039/c0mb00015a. Link to article on publisher's site. Epub 2010 Jul 6.


At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed