| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1356107 | Bioorganic Chemistry | 2012 | 7 Pages |
A series of bi- and tricyclic β-lactam compounds was synthesized and evaluated as inhibitors of cleavage of synthetic substrates in vitro by the serine proteases Human Leukocyte Elastase (HLE), Human Leukocyte Proteinase 3 (HLPR3) and Porcine Pancreatic Elastase (PPE). The obtained results have permitted us to describe a homobenzocarbacephem compound as HLE and HLPR3 inhibitor, to observe the positive effect that the styryl group exerts on the HLE inhibitory activity in polycyclic β-lactam compounds and to conclude that the hydroxyl function decreases the HLE inhibitory activity or rules it out completely.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► A series of bi- and tricyclic β-lactam compounds has been synthesized. ► They have been evaluated as inhibitors of Human Leukocyte and Porcine Pancreatic Elastases and Human Leukocyte Proteinase 3. ► A homobenzocarbacephem compound has been described as HLE and HLPR3 inhibitor. ► The styryl group exerts a positive effect on the HLE inhibitory activity. ► The hydroxyl function decreases or eliminates the HLE inhibitory activity.
