Abstract
A modification of novel fluorinated organophosphorous compounds containing terminal alkyne group by different azidopeptides via Cu(I)-catalyzed click chemistry has been described. The inhibitor activity of trifluoromethyl-containing methylphosphonates and their peptide-conjugates towards acetylcholinesterase, butyrylcholinesterase, and carboxylesterase has been investigated. It was shown that the incorporation of peptide fragments significantly modulates the esterase profile of starting methylphosphonates.
Copyright © 2011 Elsevier Ltd. All rights reserved.
MeSH terms
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Carboxylesterase / antagonists & inhibitors
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Catalysis
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Cholinesterase Inhibitors / chemical synthesis
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Cholinesterase Inhibitors / chemistry
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Cholinesterase Inhibitors / pharmacology
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Click Chemistry
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Enzyme Activation / drug effects
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Fluorine / chemistry
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Inhibitory Concentration 50
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Molecular Structure
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Organophosphonates / chemical synthesis*
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Organophosphonates / chemistry
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Organophosphonates / pharmacology
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Peptides / chemical synthesis*
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Peptides / chemistry
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Peptides / pharmacology
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Serine Proteinase Inhibitors / chemical synthesis*
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Serine Proteinase Inhibitors / pharmacology
Substances
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Cholinesterase Inhibitors
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Organophosphonates
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Peptides
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Serine Proteinase Inhibitors
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Fluorine
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Carboxylesterase