Abstract
Protein arginin deaminase 4 (PAD4) is a calcium dependent enzyme which catalyses the conversion of peptidyl-arginine into peptidyl-citrulline and is implicated in several diseases such as rheumatoid arthritis (RA) and cancer. Herein we report the discovery of novel small-molecule, non peptidic PAD4 inhibitors incorporating primary/secondary guanidine moieties.
Copyright © 2012 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Enzyme Activation / drug effects
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Guanine / chemistry
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Humans
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Hydrolases / antagonists & inhibitors*
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Inhibitory Concentration 50
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Models, Molecular
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Molecular Structure
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Protein-Arginine Deiminase Type 4
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Protein-Arginine Deiminases
Substances
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Enzyme Inhibitors
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Guanine
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Hydrolases
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PADI4 protein, human
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Protein-Arginine Deiminase Type 4
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Protein-Arginine Deiminases