Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10588357 | Bioorganic & Medicinal Chemistry Letters | 2012 | 5 Pages |
Abstract
The synthesis, inhibitory activity and mode of action of oxazolidine-2,4-diones against porcine pancreatic elastase, here used as a model for human neutrophil elastase, are reported. The nature of N-substitution at the oxazolidine-2,4-dione scaffold has large effect on the inhibitory potency against elastase. N-Acyl and N-sulfonyloxazolidine-2,4-diones emerged as potent pseudo-irreversible inhibitors, displaying high second-order rate constants for PPE inactivation. The title compounds were also shown to be potent inhibitors of human neutrophil elastase (HNE) and proteinase-3, and weak inhibitors of human cathepsin G. The results herein presented show that the oxazolidine-2,4-diones represent a new promising class of serine protease inhibitors.
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Ana Bela Santana, Susana D. Lucas, LÃdia M. Gonçalves, Henrique F. Correia, Teresa A.F. Cardote, Rita C. Guedes, Jim Iley, Rui Moreira,