Proteases are enzymes which hydrolytically cleave peptide bonds at specific amino acid residues in proteins. They play many important biological roles associated with human disease, such as in cancer metastasis, viral infection, and certain neurological disorders. Thus, protease inhibitors make up a whole class of pharmaceutical compounds. A library of enaminones with amino acid functional groups was analyzed for its effects on protease activity. The 31 synthesized compounds underwent screening against four different purified proteases (bromelain, trypsin, chymotrypsin, and protease A) to determine their effects on proteolytic activity using BSA as a substrate. A few compounds demonstrated both activation and inhibition of protease activity, especially when utilizing bromelain. This capacity for modulating protease activity suggests that some of the enaminones might have biological activity and serve as promising intermediates for the synthesis of novel compounds with therapeutic potential.

Effects of an enaminone library with amino acid functionalities on protease activities

245th National Meeting (2013)

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