Abstract
Prototype irreversible inhibitors of the cysteinyl protease Der p I were designed, synthesised and evaluated in vitro. Candidates were designed using a modular approach, whereby a peptide sequence was appended with known thiophilic moieties. This hinged on utilizing peptide sequences from substrate specificity data compiled using proprietary RAPiD technology.
MeSH terms
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Animals
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Antigens, Dermatophagoides
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B-Lymphocytes
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Cell Line
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Cysteine Endopeptidases / metabolism*
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Cysteine Proteinase Inhibitors / chemical synthesis*
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Cysteine Proteinase Inhibitors / chemistry
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Cysteine Proteinase Inhibitors / pharmacology
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Drug Design
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Feces
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Glycoproteins / antagonists & inhibitors*
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Glycoproteins / isolation & purification
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Humans
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Mites / enzymology
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Mites / immunology
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Molecular Structure
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Structure-Activity Relationship
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Substrate Specificity
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Sulfones / chemical synthesis*
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Sulfones / chemistry
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Sulfones / pharmacology
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Vinyl Compounds / chemical synthesis
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Vinyl Compounds / chemistry
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Vinyl Compounds / pharmacology
Substances
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Antigens, Dermatophagoides
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Cysteine Proteinase Inhibitors
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Glycoproteins
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Sulfones
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Vinyl Compounds
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Cysteine Endopeptidases