Please sign in to download the files. A new tab will open where you can login/register.


Protease Targeted Library

Proteases (also known as peptidases or proteinases) are a subgroup of hydrolase enzymes that catalyze proteolysis. There are two main subtypes of proteases: exoproteases that cleave peptide bonds at the terminus of polypeptide chains and endoproteases that act internally by finding out a site of interaction. Proteases are also classified according to their catalytic site, forming four major classes:

Proteases take part in a variety of physiological processes and represent potential drug targets for various diseases (cardiovascular disorders, cancer, arthritis, atherosclerosis), as well as for combating many viruses and parasites (AIDS, malaria, Chagas disease, leishmaniasis, or African sleeping sickness) [1-6].

Life Chemicals has designed a dedicated selection of 5,700 potential protease inhibitors applying both ligand-based and receptor-based approaches.

The compound selection can be customized based on your requirements, cherry picking is available.

Please, contact us at for any additional information and price quotations.


Compound selection

A reference set of 80,000 unique molecules with protease inhibitor activity from the ChEMBL database that contained substances with their activity less than 10 uM was first prepared. A 2D fingerprint similarity search against the reference compound set provided about 5,700 structurally-diverse screening compounds selected from Life Chemicals HTS Compound Collection (Fig. 1). PAINS, toxic and reactive compounds are excluded from the Library.

Several customized dockings were carried out against separate targets. All simulations, including flexible and covalent docking and compound optimization to Cathepsin B, were done with Sybyl-X software.

The list of protease targets used for the Library preparation is represented below:

  • 26S proteasome non-ATPase regulatory subunit 14
  • ADAM (17, S4, S5)
  • Alpha-chymotrypsin
  • Aminopeptidase N
  • Angiotensin-converting enzyme
  • Anthrax lethal factor
  • ATP-dependent Clp protease
  • Beta-secretase 1
  • Botulinum neurotoxin type A
  • CAAX prenyl protease 1
  • Calpain 1 and 2
  • Carboxypeptidase A1 and B2
  • Caspase (1, 3, 5-7)
  • Cathepsin (B, K, L, S)
  • Coagulation factor X and XII
  • Collagenase
  • Cruzipain
  • Cysteine protease falcipain 2 and 3
  • Cystinyl aminopeptidase
  • Dipeptidyl peptidase II and IV
  • Endoplasmic reticulum aminopeptidase 1 and 2
  • Endothelin-converting enzyme 2
  • Endothiapepsin
  • Enteropeptidase
  • Epoxide hydratase
  • Gamma-secretase
  • Glutamate carboxypeptidase II
  • Hepatitis C virus NS3 protease/helicase
  • Hepatitis C virus polyprotein
  • HIV type 1 protease
  • Kallikrein 7
  • Legumain
  • Leukocyte elastase
  • Leukocyte proteinase 3
  • Leukotriene A4 hydrolase
  • Lysosomal Pro-X carboxypeptidase
  • Matriptase
  • Matrix metalloproteinase (1-3, 8-9, 12-13)
  • Membrane-bound transcription factor site-1 protease
  • Methionine aminopeptidase 1, 2
  • Neprilysin
  • Plasma kallikrein
  • Plasmepsin 2
  • Plasminogen
  • Prenyl protein-specific protease
  • Prolyl endopeptidase
  • Proteasome Macropain subunit MB1
  • Puromycin-sensitive aminopeptidase
  • Renin
  • Sentrin-specific protease 1, 6-8
  • Seprase
  • Serine protease hepsin
  • Thermolysin
  • Thrombin
  • Tripeptidyl aminopeptidase
  • Trypsin
  • Tryptase beta-1
  • Ubiquitin carboxyl-terminal hydrolase 1, 2, 7, L3
  • Urokinase-type plasminogen activator
  • Zinc aminopeptidase

Compound analogs from the Protease Targeted Library similar to the known protease inhibitors (CHEMBL)

Figure 1. Compound analogs from the Protease Targeted Library similar to the known protease inhibitors (CHEMBL).



  1. Tavano, O. L.; Berenguer-Murcia, A.; Secundo, F.; Fernandez-Lafuente, R. Biotechnological Applications of Proteases in Food Technology. Compr. Rev. Food Sci. Food Saf. 2018, 17 (2), 412–436.
  2. Harish, B. S.; Uppuluri, K. B. Microbial Serine Protease Inhibitors and Their Therapeutic Applications. International Journal of Biological Macromolecules. Elsevier B.V. February 1, 2018, pp 1373–1387.
  3. Drag, M.; Salvesen, G. S. Emerging Principles in Protease-Based Drug Discovery. Nature Reviews Drug Discovery. Nature Publishing Group 2010, pp 690–701.
  4. Hellinger, R.; Gruber, C. W. Peptide-Based Protease Inhibitors from Plants. Drug Discovery Today. Elsevier Ltd September 1, 2019, pp 1877–1889.
  5. Ruf, W. Proteases, Protease-Activated Receptors, and Atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 2018, 38 (6), 1252–1254.
  6. Agbowuro, A. A.; Huston, W. M.; Gamble, A. B.; Tyndall, J. D. A. Proteases and Protease Inhibitors in Infectious Diseases. Medicinal Research Reviews. John Wiley and Sons Inc. July 1, 2018, pp 1295–1331.
This site uses cookies. Some of these cookies are essential, while others help us improve your experience by providing insights into how the site is being used. By using our website, you accept our conditions of use of cookies to track data and create content (including advertising) based on your interest. Accept