Metalloenzyme and Chelator Focused Libraries

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. 

Please, contact us at for any details and quotations.


  1. 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.
  2. 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.
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