Protease inhibitors
Protease inhibitors are molecules which protein- cleaving enzymes , the peptidases (old name: proteases), inhibit and thus prevent the breakdown of proteins .
properties
Natural protease inhibitors are often peptides or proteins themselves . In addition, low molecular weight substances can also inhibit the function of peptidases. The body's own protease inhibitors regulate the function of peptidases. Some scorpion and snake poisons contain protease inhibitors, which are partly responsible for their toxicity . In the drug therapy , in particular protease inhibitors to be viral peptidases as drugs used, which, like the HIV protease inhibitors or HCV protease inhibitors , as antiviral agents for the treatment of HIV infections or HCV serve infections. In addition, protease inhibitors directed against the body's own proteases are used, for example, as anticoagulants or antihypertensive agents.
There are four classes of proteases according to their structure and active center , which can be inhibited differently . In biochemistry , different protease inhibitors are used in the course of protein purification , sometimes as a mixture. However, due to their toxicity, some of these can only be used in vitro .
Serine proteases are inhibited by:
Cysteine proteases are inhibited by:
- E-64 and iodoacetamide
Metalloproteases are inhibited by:
Aspartate proteases are inhibited by:
Leupeptin and alpha-2 macroglobulin inhibit several classes.
literature
- Abbenante G, Fairlie DP: Protease inhibitors in the clinic . In: Med Chem . 1, No. 1, January 2005, pp. 71-104. PMID 16789888 .
Individual evidence
- ↑ W. Kaim / B. Schwederski, Bioinorganische Chemie, Teubner Study Books, 1995, ISBN 3-519-13505-1 , p. 261
