Abstract
A random screening approach has identified 2-chloro-3-substituted-1,4-naphthoquinones as potent inactivators of HCMV protease. Enzyme inactivation is due to modification of Cys202. Two of the most potent compounds maintain activity against HCMV in a plaque reduction assay.
MeSH terms
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Binding Sites
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Cell Line
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Cysteine / chemistry
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Glutathione / chemistry
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Humans
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Leukocyte Elastase / metabolism
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Molecular Structure
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Naphthoquinones / chemical synthesis*
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Naphthoquinones / pharmacology
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Serine Endopeptidases / metabolism*
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Serine Proteinase Inhibitors / chemical synthesis*
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Serine Proteinase Inhibitors / pharmacology
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Thrombin / metabolism
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Viral Plaque Assay
Substances
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Naphthoquinones
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Serine Proteinase Inhibitors
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Serine Endopeptidases
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assemblin
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Leukocyte Elastase
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Thrombin
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Glutathione
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Cysteine
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1,4-naphthoquinone