Identification and characterization of peptide probes directed against PKCα conformations

S. Salman Ashraf, E. Anderson, Z. Fredericks, K. Duke, P. T. Hamilton

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Phage display is a powerful technology that allows identification of high affinity peptides that bind specifically to a given molecular target. Using a highly complex peptide display library, we have identified separate classes of peptides that bind to protein kinase C alpha (PKCα) only under activation conditions. Furthermore, peptide binding was specific to PKCα and not to any of the other closely related PKC isoforms. The conformational and isoform specificity of the peptide binding was demonstrated using surface plasmon resonance as well as time-resolved fluorescence assays. Kinase assays showed that these peptides were not direct substrates for PKC nor did they inhibit phosphorylation of PKC substrates. These peptides are most likely directed against protein-protein interaction sites on PKC. The data presented here offers another example of application of phage display technology to identify conformation-dependent peptide probes against therapeutically important drug targets. These peptides are ideally suited to be used as surrogate ligands to identify compounds that bind specifically to PKCα, as well as conformational probes to detect activated forms of PKCα.

Original languageEnglish
Pages (from-to)263-273
Number of pages11
JournalJournal of Peptide Research
Issue number5
Publication statusPublished - May 1 2003
Externally publishedYes


  • Conformational probes
  • Peptide phage display
  • Protein kinase C
  • Surrogate ligands

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology


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