Proteases (proteinases or peptidases) are a class of enzymes that catalyze proteolysis, breakdown of proteins into smaller polypeptides or single amino acids by cleaving peptide bonds via hydrolysis. Proteases are involved in many biological functions, such as cell signaling, protein catabolism (the breakdown of old proteins), and digestion of ingested proteins.
Proteinases are considered promising drug targets for diseases ranging from cardiovascular disorders to cancer and, what is more, combating many parasites and viruses. Nonetheless, drug development for new protease targets has recently turned out to be rather challenging due to various factors, in particular, the difficulty of achieving selectivity when targeting protease active sites .
Protease inhibitors typically feature specialized moieties that specifically interact with catalytic residues in the active center to mimic the peptide substrates of the target enzymes. Such moieties may consist of electrophilic warheads e.g. Michael acceptors, epoxyketones, β-lactams or β-lactones that are attacked by active site nucleophiles and generate covalent adducts .
Life Chemicals offers a proprietary collection of drug-like screening compounds with predicted protease inhibitory activity to facilitate protease-based drug discovery efforts. Potential protease-targeted modulators were selected, using both ligand-based (computational chemistry, 2D fingerprint similarity search) and receptor-based (high-throughput virtual screening, flexible and covalent docking) approaches.
The compound selection can be customized based on your requirements, cherry picking is available.
Please, contact us at firstname.lastname@example.org for any additional information and price quotations.
- Drag, M.; Salvesen, G. S. Emerging Principles in Protease-Based Drug Discovery. Nature Reviews Drug Discovery. Nature Publishing Group 2010, pp 690–701. https://doi.org/10.1038/nrd3053.
- L. Kaysser. Built to bind: Biosynthetic strategies for the formation of small-molecule protease inhibitors. Nat. Prod. Rep., vol. 36, no. 12, pp. 1654–1686, 2019, doi: 10.1039/c8np00095f.