2. Recombinant Proteins
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  4. Protease Inhibitors

Protease Inhibitors

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Many biological functions rely upon proteases, including food digestion, lysosomal degradation, and signaling cascades. Since proteases trigger an irreversible event, the hydrolysis of a protein, their activity must be tightly controlled. An extensive regulatory network of protease inhibitors has evolved to ensure targeted spatial and temporal control of their activity. Naturally occurring protease inhibitors (antiproteases) are usually proteins or peptides, which control proteolysis within an organism, as well as inactivate proteases of competing or predatory species. Protease inhibitors can be further classified into 5 groups (serine, threonine, cysteine, aspartyl and metalloprotease inhibitors) according to the mechanism employed at the active site of proteases they inhibit. Some protease inhibitors interfere with more than one type of protease. For example, the serine family of protease inhibitors (serpins) is generally known as active against serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified.

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