proteaseremmers

Protease inhibitors, or protease inhibitors (proteaseremmers in Danish), are molecules that bind proteases to reduce proteolytic activity. They can be endogenous (produced by organisms) or exogenous (drugs, food additives). They include small molecules and proteins, and they regulate proteolysis in processes such as digestion, immune defense, blood coagulation, and tissue remodeling.

Inhibition may occur by occupying the protease active site (competitive inhibition), binding at a different site to change enzyme activity (noncompetitive inhibition), or forming irreversible covalent complexes. Proteases span serine, cysteine, aspartic, and metalloproteases. Endogenous inhibitors include serpins (for example, alpha1-antitrypsin), cystatins, TIMPs (tissue inhibitors of metalloproteinases), and alpha2-macroglobulin. Drugs include HIV and HCV protease inhibitors such as ritonavir, saquinavir, boceprevir, and telaprevir.

Protease inhibitors help regulate digestion, coagulation, immune responses, signaling, and extracellular matrix remodeling. When proteolysis is misregulated, it can contribute to diseases such as emphysema, arthritis, cancer, or chronic viral infections. Therapeutic inhibitors must balance efficacy with potential side effects and the possibility of resistance, particularly in rapidly mutating viruses.

In medicine, inhibitors are used to treat infections and some cancers; in research, they help study protease function; and in biotechnology they stabilize proteins and prevent unwanted proteolysis during production. Ongoing development aims to improve selectivity, potency, pharmacokinetics, and safety.