Abstract
Dipeptide-based sulfonium peptidylmethylketones derived from 6-diazo-5-oxo-L-norleucine (DON) have been investigated as potential water-soluble inhibitors of extracellular transglutaminase. The lead compounds were prepared in four steps and exhibited potent activity against tissue transglutaminase.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Catalytic Domain
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Chemistry, Pharmaceutical / methods
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Diazooxonorleucine / chemistry*
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Drug Design
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Ethanol / chemistry
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GTP-Binding Proteins / antagonists & inhibitors*
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Humans
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Inhibitory Concentration 50
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Ketones / chemistry
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Magnetic Resonance Spectroscopy
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Mass Spectrometry / methods
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Peptides / chemistry
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Protein Glutamine gamma Glutamyltransferase 2
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Solubility
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Spectrophotometry / methods
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Transglutaminases / antagonists & inhibitors*
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Water / chemistry*
Substances
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Ketones
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Peptides
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Diazooxonorleucine
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Water
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Ethanol
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Protein Glutamine gamma Glutamyltransferase 2
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Transglutaminases
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GTP-Binding Proteins