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.
Original language | English |
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Pages (from-to) | 9808-9812 |
Number of pages | 5 |
Journal | Organic and Biomolecular Chemistry |
Volume | 13 |
Issue number | 38 |
Early online date | 4 Aug 2015 |
DOIs | |
Publication status | Published - Oct 2015 |
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry
- Biochemistry
- General Medicine