Catechol-based matrix metalloproteinase inhibitors with additional antioxidative activity. (4th November 2016)

• Record Type: Journal Article
• Authors: Tauro, Marilena; Laghezza, Antonio; Loiodice, Fulvio; Piemontese, Luca; Caradonna, Alessia; Capelli, Davide; Montanari, Roberta; Pochetti, Giorgio; Di Pizio, Antonella; Agamennone, Mariangela; Campestre, Cristina; Tortorella, Paolo
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 31(2016.)Supplement 4
• Page Start: 25
• Page End: 37
• Publication Date: 2016-11-04
• Subjects: Antioxidants -- inhibitors -- metalloenzymes -- structure–activity relationships -- X-ray crystallography; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2016.1217853
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract: New catechol-containing chemical entities have been investigated as matrix metalloproteinase inhibitors as well as antioxidant molecules. The combination of the two properties could represent a useful feature due to the potential application in all the pathological processes characterized by increased proteolytic activity and radical oxygen species (ROS) production, such as inflammation and photoaging. A series of catechol-based molecules were synthesized and tested for both proteolytic and oxidative inhibitory activity, and the detailed binding mode was assessed by crystal structure determination of the complex between a catechol derivative and the matrix metalloproteinase-8. Surprisingly, X-ray structure reveals that the catechol oxygens do not coordinates the zinc atom.