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pubmed-article:11327577pubmed:abstractTextPotent and selective inhibition of matrix metalloproteinases was demonstrated for a series of sulfonamide-based hydroxamic acids. The design of the heterocyclic sulfonamides incorporates a six- or seven-member central ring with a P2' substituent that can be modified. Binding interactions of this substituent at the S2' site are believed to contribute to high inhibitory potency against stromelysin, collagenase-3 and gelatinases A and B, and to provide selectivity against collagenase-1 and matrilysin. An X-ray structure of a stromelysin inhibitor complex was obtained to provide insights into the SAR and selectivity trends observed for the series.lld:pubmed
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pubmed-article:11327577pubmed:articleTitleHeterocycle-based MMP inhibitors with P2' substituents.lld:pubmed
pubmed-article:11327577pubmed:affiliationProcter and Gamble Pharmaceuticals, Health Care Research Center, Mason, OH 45040, USA. spikul@avalonrx.comlld:pubmed
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