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.
2010 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Histone-Lysine N-Methyltransferase / antagonists & inhibitors
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Histone-Lysine N-Methyltransferase / metabolism
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Humans
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Inhibitory Concentration 50
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Methylation
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Protein-Arginine N-Methyltransferases / antagonists & inhibitors*
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Protein-Arginine N-Methyltransferases / metabolism*
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Repressor Proteins / antagonists & inhibitors
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Repressor Proteins / metabolism
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S-Adenosylmethionine / analogs & derivatives*
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S-Adenosylmethionine / pharmacology*
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Substrate Specificity
Substances
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Repressor Proteins
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S-Adenosylmethionine
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PRMT1 protein, human
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Protein-Arginine N-Methyltransferases
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Histone-Lysine N-Methyltransferase
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SETD7 protein, human