Development of artificial peptidase domains

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Although artificial proteases with novel substrate specificities and unique catalytic properties would have potential utility in useful analytical methods and new therapeutic approaches, de novo creation of artificial protease domain has never achieved. This program aims at development of artificial small peptidase domains, which catalyzes self-cleavage of an amide bond.By using the translation initiation reprogramming method, a short (20-40 aa length) random peptide library with a 1013 diversity was prepared. In vitro selection experiments of active species from the resulting peptide library has provided 22 novel peptide sequences that could exhibit the desired self-cleavage activity.