Trypsin, therapeutic enzyme

The lability of host defense peptides to proteases and peptidases has been investigated as a method for increasing the therapeutic efficacy of these molecules. The high concentration of basic residues in host defense peptides increases the lability of these molecules to endogenous trypsin-like enzymes and represents a significant therapeutic impediment. As host defense peptides are significantly sensitive to proteases, with half-lives of minutes in vivo, peptides that are protease resistant while retaining activity would offer a potential resolution to this problem. 

A novel concept of using bioadhesive polymers as enzyme inhibitors has been developed [97]. Included are derivatives of poly acrylic acid, polycarbophil, and car-bomer to protect therapeutically important proteins and peptides from proteolytic activity of enzymes, endopeptidases (trypsin and a-chymotrypsin), exopeptidases (carboxypeptidases A and B), and microsomal and cytosolic leucine aminopeptidase. However, cysteine protease (pyroglutamyl aminopeptidase) is not inhibited by polycarbophil and carbomer [97]. 

A09A A Enzyme Preparations Enzymes can be used therapeutically. Some are of animal origin (from the stomach and pancreas of food animals), some of vegetable origin and others of microbiological origin. Examples of the first type include pepsin and pancreatin, a mixture of amylase, lipase and trypsin (a protease) which catalyses the metabolism of proteins into smaller peptides and amino-acids. Pancreatin is frequently prescribed for patients with cystic fibrosis. 

Some researchers point out that, after a thorough study of specific properties of certain proteolytic enzymes has been made, one can expect to increase their potential therapeutic activity. In 1971 Prof. M.M. Krasnov reported that a specific protease which normally destroys kallikrein and trypsin... 

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