http://www.cnr.it/ontology/cnr/individuo/prodotto/ID265787
Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold (Articolo in rivista)
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- Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold (Articolo in rivista) (literal)
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- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/ml300446a (literal)
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Mori, Mattia; Massaro, Assunta; Calderone, Vito; Fragai, Marco; Luchinat, Claudio; Mordini, Alessandro (2013)
Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold
in ACS medicinal chemistry letters; AMER CHEMICAL SOC, WASHINGTON (Stati Uniti d'America)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Mori, Mattia; Massaro, Assunta; Calderone, Vito; Fragai, Marco; Luchinat, Claudio; Mordini, Alessandro (literal)
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- Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
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Università di Firenze
ICCOM-CNR (literal)
- Titolo
- Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold (literal)
- Abstract
- A new class of potent matrix metalloproteinase (MMP) inhibitors designed by structure-based optimization of the well-known arylsulfonamide scaffold is presented. Mols. show an ethylene linker connecting the sulfonamide group with the P1' arom. portion and a D-proline residue bearing the zinc-binding group. The affinity improvement provided by these modifications led us to discover a nanomolar MMP inhibitor bearing a carboxylate moiety as zinc-binding group, which might be a promising lead mol. Notably, a significant selectivity for MMP-8, MMP-12, and MMP-13 was obsd. with respect to MMP-1 and MMP-7. (literal)
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