Abstract
A novel 17-mer peptide ligand for cyclic AMP was designed using the amino acid sequences of essential subsites in various cyclic AMP-dependent protein kinase (protein kinase A) families. The Au disk electrode, which was modified with the designed 17-mer oligopeptide, responded to cyclic AMP but virtually did not respond to any other cyclic nucleotides using the ion channel sensor mechanism. On the other hand, a scrambled peptide, which had the same amino acid composition as and had an amino acid sequence different from the 17-mer oligopeptide, did not respond to any nucleotides. This indicates that the designed 17-mer peptide actually acted as a selective ligand for cyclic AMP. This ligand-designing strategy using peptide sequences in target-binding proteins may possibly be extended to the design of peptide ligands for other second messengers.
Original language | English |
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Pages (from-to) | 4671-4674 |
Number of pages | 4 |
Journal | Analytical chemistry |
Volume | 72 |
Issue number | 19 |
DOIs | |
Publication status | Published - Oct 1 2000 |
All Science Journal Classification (ASJC) codes
- Analytical Chemistry