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A dual functional peptide carrying in vitro selected catalytic and binding activities
OAI: oai:purehost.bath.ac.uk:publications/f378da10-040c-4311-a523-67a7340030a6 • DOI: https://doi.org/10.1039/c5ob01271f
Abstract
When minimal functional sequences are used, it is possible to integrate multiple functions on a single peptide chain, like a "single stroke drawing". Here a dual functional peptide was designed by combining in vitro selected catalytic and binding activities. For catalytic activity, we performed in vitro selection for a peptide aptamer binding to hemin by using ribosome display and isolated a peptide that had peroxidase activity in the presence of hemin. By combining the selected catalytic peptide with a peptide antigen, which can be recognized by an antibody, an enzyme-antibody conjugate-like peptide was obtained. This study demonstrates a successful strategy to create dual functionalized peptide chains for use in immunoassays.