Metalloproteases, also known as metalloproteinases, are a class of protease enzymes whose catalytic mechanism involves a metal ion. For their biological activity metalloproteases require a divalent cation (usually zinc, but sometimes cobalt) that activates a water molecule in their active site. This enzyme family includes matrix metallopeptidases (matrixins), calcium-dependent zinc-containing endopeptidases, capable of extracellular matrix protein degradation and processing a number of bioactive molecules. MMPs are promising protein targets for drug discovery against cancer, neurodegenerative diseases, inflammation, and other pathologies. Several small-molecule chelators have been shown to inhibit metalloproteins effectively [1-2].
Life Chemicals has prepared a careful selection of drug-like screening compounds with metal-chelating moieties and potential metalloenzyme inhibitors to facilitate HTS and FBDD.
Compound cherry-picking within each screening library is available. Custom compound selection based on specific parameters can be performed, with the most convenient terms and competitive pricing provided.
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- Jacobsen FE, Lewis JA, Cohen SM. A new role for old ligands: discerning chelators for zinc metalloproteinases. J Am Chem Soc. 2006 Mar 15;128(10):3156-7. DOI: 10.1021/ja057957s. PMID: 16522091.
- Puerta DT, Lewis JA, Cohen SM. New beginnings for matrix metalloproteinase inhibitors: identification of high-affinity zinc-binding groups. J Am Chem Soc. 2004 Jul 14;126(27):8388-9. DOI: 10.1021/ja0485513. PMID: 15237990.