Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases.

Abstract

Prototype inhibitors of protein arginine methyltransferases (PRMTs) have been constructed by attaching guanidine functionality via a variable linker to non-reactive amine analogues of the cellular co-factor (S)-adenosyl methionine (AdoMet). Potent inhibition of PRMT1 (IC(50) of approximately 3-6 microM) combined with weak inhibition of the lysine methyltransferase SET7 (approximately 50% of activity at 100 microM) was observed for two such compounds.

DOI: 10.1016/j.bmcl.2010.02.069

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@article{Dowden2010TowardTD, title={Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases.}, author={James Dowden and W. David Hong and Richard V Parry and Richard Pike and Stephen Geoffrey Ward}, journal={Bioorganic & medicinal chemistry letters}, year={2010}, volume={20 7}, pages={2103-5} }