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

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 approac...

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Bibliographic Details
Published in:Molecular bioSystems 2011-01, Vol.7 (1), p.48-51
Main Authors: Bicker, Kevin L, Obianyo, Obiamaka, Rust, Heather L, Thompson, Paul R
Format: Article
Language:English
Subjects:
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
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Summary: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.
ISSN:1742-206X
1742-2051
DOI:10.1039/c0mb00015a