344596-80-1Relevant academic research and scientific papers
Discovery of a new class of potent MMP inhibitors by structure-based optimization of the arylsulfonamide scaffold
Mori, Mattia,Massaro, Assunta,Calderone, Vito,Fragai, Marco,Luchinat, Claudio,Mordini, Alessandro
, p. 565 - 569 (2013)
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.
