59922-33-7Relevant articles and documents
Matrix metalloproteinase inhibitors containing a (carboxyalkyl)amino zinc ligand: Modification of the P1 and P2' residues
Brown,Brown,Bickett,Chambers,Davies,Deaton,Drewry,Foley,McElroy,Gregson,McGeehan,Myers,Norton,Salovich,Schoenen,Ward
, p. 674 - 688 (2007/10/02)
Systematic modification of the presumed P1 side chain in a series of (carboxyalkyl)amino-based inhibitors of matrix metalloproteinases enabled identification of the 2-(1,3-dihydro-1,3-dioxo-2H-benz[f]isoindol-2-yl)ethyl group as a preferred substituent imparting potent inhibition of the enzymes collagenase and gelatinase. It was subsequently found that the P2'-P3' residues in this series could be replaced by small non-peptide residues, while maintaining inhibitory potency. The imide group in this series of compounds can undergo autocatalytic hydrolysis under neutral conditions.
