Journal of the American Chemical Society · 2010 · 118 citations · 8 references
PharmacyChemistryMedicinal ChemistryDrug DesignDrug DiscoveryEnzymologyBioinorganic ChemistryEnzyme InhibitionFragment-based Lead DiscoveryLead Compound DesignLead DiscoveryLigand BindingFragment Screening LibrariesMatrix Metalloproteinase InhibitorsMatrix MetalloproteinasesMetal Ion InhibitionMetalloenzyme DiscoveryMetalloprotease MechanismZinc EnzymesZinc-dependent Enzymes
Derived from the extensive work in the area of small molecule zinc(II) ion sensors, chelating fragment libraries of quinoline- and benzimidazole-sulfonamides have been prepared and screened against several different zinc(II)-dependent matrix metalloproteinases (MMPs). The fragments show impressive inhibition of these metalloenzymes and preferences for different MMPs based on the nature of the chelating group. The findings show that focused chelator libraries are a powerful strategy for the discovery of lead fragments for metalloprotein inhibition.
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Zinc‐Binding Groups Modulate Selective Inhibition of MMPs
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The Design of Inhibitors for Medicinally Relevant Metalloproteins
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