Protease Inhibitors

Protease Inhibitors

Published on 19/02/2019

Protease inhibitors are molecules that inhibit protease function by binding either reversibly or irreversibly to the enzyme.

The majority of proteases can be roughly classified into seven types that are defined by their key catalytic amino acid residue, and thus differ in the way they catalyze the cleavage of peptide bonds. Consequently, most inhibitors are only active against one or two types of proteases.


Inhibitors block protease function.

The activity of proteases is strictly regulated in all organisms. This tight control is disrupted by cell lysis. Thus, when attempting to extract and isolate proteins from cells, it is necessary to inhibit protease function in order to avoid the degradation of target proteins. We offer a selection of individual protease inhibitors which are suitable for the protection of proteins during their extraction from cultured cells, microorganisms, as well as animal and plant tissues.


  • Isolation and Characterization of E–64, a New Thiol Protease Inhibitor; K. Hanada, M. Tamai, M. Yamagishi, S. Ohmura, J. Sawada and I. Tanaka; Agricultural and Biological Chemistry 2014; 42: 523-528. doi:10.1080/00021369.1978.10863014
  • Structural basis of inhibition of cysteine proteases by E-64 and its derivatives; K. Matsumoto, K. Mizoue, K. Kitamura, W. C. Tse, C. P. Huber and T. Ishida; Biopolymers 1999; 51: 99-107. doi:10.1002/(SICI)1097-0282(1999)51:13.0.CO;2-R
  • Degradation and disposal of some enzyme inhibitors; G. Lunn and E. B. Sansone; Appl Biochem Biotechnol 1994; 48: 57-59. doi:10.1007/bf02796162
  • [8] Maintaining protein stability; M. P. Deutscher; Methods in enzymology M. P. Deutscher 1990; 182: 83-89. doi:
  • Active and inactive forms of the transition-state analog protease inhibitor leupeptin: explanation of the observed slow binding of leupeptin to cathepsin B and papain; R. M. Schultz, P. Varma-Nelson, R. Ortiz, K. A. Kozlowski, A. T. Orawski, P. Pagast and A. Frankfater; J Biol Chem 1989; 264: 1497-507.
  • Mode of binding of E-64-c, a potent thiol protease inhibitor, to papain as determined by X-ray crystal analysis of the complex; K. Matsumoto, D. Yamamoto, H. Ohishi, K. Tomoo, T. Ishida, M. Inoue, T. Sadatome, K. Kitamura and H. Mizuno; FEBS Letters 1989; 245: 177-180. doi:10.1016/0014-5793(89)80216-9
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  • Synthetic low molecular weight inhibitors of serum kallikrein; F. Markwardt, J. Drawert and P. Walsmann; Biochem Pharmacol 1974; 23: 2247-56. doi:
  • Use Of Benzamidine to Prevent The Destruction Of Thyrotropin-Releasing Hormone (TRH) By Blood; S. L. Jeffcoate and N. White; The Journal of Clinical Endocrinology & Metabolism 1974; 38: 155-157. doi:10.1210/jcem-38-1-155 %J The Journal of Clinical Endocrinology & Metabolism
  • Letter: A thermolysin inhibitor produced by Actinomycetes: phospholamidon; H. Suda, T. Aoyagi, T. Takeuchi and H. Umezawa; The Journal of antibiotics 1973; 26: 621-3.
  • Irreversible enzyme inhibitors. 180. Irreversible inhibitors of the C'la component of complement derived from m-(phenoxypropoxy)benzamidine and phenoxyacetamide; B. R. Baker and M. Cory; J Med Chem 1971; 14: 119-25. doi:10.1021/jm00284a009
  • Pepstatin, a new pepsin inhibitor produced by Actinomycetes; H. Umezawa, T. Aoyagi, H. Morishima, M. Matsuzaki and M. Hamada; The Journal of antibiotics 1970; 23: 259-62.
  • The Action Of Phenylmethylsulfonyl Fluoride On Human Acetylcholinesterase, Chymotrypsin And Trypsin; P. Turini, S. Kurooka, M. Steer, A. N. Corbascio and T. P. Singer; Journal of Pharmacology and Experimental Therapeutics 1969; 167: 98.
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