Abstract
A series of N-arylsulfonyl S-alkyl homocysteine hydroxamic acids were synthesized with variations in three subsites corresponding to P(1), P(1)', and P(2)'. Enzyme assays with a variety of MMPs revealed activity at the low nanomolar level.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Collagenases / chemistry
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Homocysteine / analogs & derivatives*
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Homocysteine / chemical synthesis*
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Homocysteine / chemistry
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Hydroxamic Acids / chemical synthesis*
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Hydroxamic Acids / chemistry
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Matrix Metalloproteinase 1 / chemistry
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Matrix Metalloproteinase 13
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Matrix Metalloproteinase 2 / chemistry
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Matrix Metalloproteinase 3 / chemistry
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Matrix Metalloproteinase 9 / chemistry
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Matrix Metalloproteinase Inhibitors
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Metalloendopeptidases / antagonists & inhibitors*
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Metalloendopeptidases / chemistry
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Models, Molecular
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / chemistry
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Protein Binding
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Structure-Activity Relationship
Substances
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Hydroxamic Acids
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Matrix Metalloproteinase Inhibitors
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Protease Inhibitors
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Homocysteine
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Collagenases
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Matrix Metalloproteinase 13
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Metalloendopeptidases
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Matrix Metalloproteinase 3
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Matrix Metalloproteinase 2
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Matrix Metalloproteinase 9
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Matrix Metalloproteinase 1