Modulation of protein-ligand interactions by photocleavage of a cyclic peptide using phosphatidylinositol 3-kinase SH3 domain as model system

Isao Takahashi, Shigeki Kuroiwa, Hanna E. Lindfors, Lionel A. Ndamba, Yoshitaka Hiruma, Tatsuo Yajima, Nobuyuki Okishio, Marcellus Ubbink, Shun Hirota

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

To photomodulate the interaction of the phosphatidylinositol 3-kinase SH3 domain with a peptide ligand, a cyclic peptide (cyclic-1)with a photolabile side chain-to-side chain linkerwas synthesized. The conformation of cyclic-1 differs from that of the parent linear peptide, but becomes identical by UV-irradiation. Accordingly, the binding affinity of cyclic-1 to the SH3 domain increased upon conversion of the cyclic to a linear flexible structure by irradiation (Kd: 3.4 ± 1.7 and 0.9 ± 0.3mM, respectively). These results confirm the usefulness of a photocleavable peptide for photocontrol of peptide-protein interactions.

Original languageEnglish
Pages (from-to)411-416
Number of pages6
JournalJournal of Peptide Science
Volume15
Issue number6
DOIs
Publication statusPublished - 2009

Keywords

  • Cyclic peptide
  • Phosphatidylinositol 3-kinase SH3 domain
  • Photocleavage
  • Photomodulation
  • Protein-peptide interaction
  • RLP1 peptide

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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