Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6228
Title: Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold
Authors: Mori, Mattia 
Massaro, Assunta
Calderone, Vito
Fragai, Marco
Luchinat, Claudio
Mordini, Alessandro
Keywords: metalloproteins
Issue Date: 2013
Project: None 
Journal: ACS MEDICINAL CHEMISTRY LETTERS
Abstract: 
A new class of potent matrix metalloproteinase (MMP) inhibitors designed by structure-based optimization of the well-known arylsulfonamide scaffold is presented. Molecules show an ethylene linker connecting the sulfonamide group with the P1′ aromatic 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 molecule. Notably, a significant selectivity for MMP-8, MMP-12, and MMP-13 was observed with respect to MMP-1 and MMP-7.
Description: 
223800
URI: http://hdl.handle.net/20.500.12779/6228
ISSN: 1948-5875
DOI: 10.1021/ml300446a
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