Abstract
The synthesis of several analogues of galardin, a MMP inhibitor, are presented with their in vitro inhibitory activity against MMP-1 and MMP-2. These compounds contain a distinct Zinc Binding Group (ZBG). Those having a 2-acylated-heterocycle as well as a 2-arylamide function do not exhibit a good inhibition/selectivity against the enzymes tested. On the contrary, those that are based on a hydrazide scaffold present potent selectivity for MMP-2 versus MMP-1.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Dipeptides / chemical synthesis*
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Dipeptides / pharmacology*
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / pharmacology
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Humans
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Inhibitory Concentration 50
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Matrix Metalloproteinase Inhibitors*
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Models, Molecular
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Structure-Activity Relationship
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Zinc / chemistry
Substances
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Dipeptides
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Enzyme Inhibitors
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Matrix Metalloproteinase Inhibitors
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N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide
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Zinc