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

Mol Biosyst. 2011 Jan;7(1):48-51. doi: 10.1039/c0mb00015a. Epub 2010 Jul 6.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Molecular Sequence Data
  • Peptide Library
  • Protein-Arginine N-Methyltransferases / antagonists & inhibitors
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Substrate Specificity

Substances

  • Enzyme Inhibitors
  • Peptide Library
  • Protein-Arginine N-Methyltransferases