| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10592138 | Bioorganic & Medicinal Chemistry Letters | 2014 | 4 Pages |
Abstract
The Mycobacterium tuberculosis extracellular zinc metalloprotease 1 (Zmp1) has been proposed to play a key role in phagosome maturation and to enhance the survival of Mycobacterium tuberculosis in the host. Consequently, small molecule inhibitors of Zmp1 are of pivotal importance as a tool to better understand the pathogenicity of Zmp1 and as lead candidates for pharmacological intervention. Here we combined in silico structure-based inhibitor design with biochemical studies to discover and characterize the first potent competitive Zmp1 inhibitor showing a Ki of 94Â nM and a high selectivity for Zmp1 with respect to human Neprilysin.
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Authors
Mattia Mori, Francesca Moraca, Davide Deodato, Davide M. Ferraris, Petra Selchow, Peter Sander, Menico Rizzi, Maurizio Botta,