Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor

Minghui Huang, Wan Ping Lai, Man Sau Wong, Mengsu Yang

Research output: Journal article publicationJournal articleAcademic researchpeer-review

11 Citations (Scopus)


A receptor binding assay based on the surface plasmon resonance (SPR) biosensor technique was developed to study the interaction between insulin-like growth factor-1 receptor (IGF-1R) and its intracellular substrate protein insulin receptor substrate-1 (IRS-1). The sensor surface was modified with anti-IGF-1R (α-subunit) monoclonal antibodies for the capturing of the receptor-containing membrane fragments from cell lysates. The IGF-1R was successfully immobilized on the sensor surface with binding capability for its intracellular substrates. SPR measurements showed that the tyrosine phosphorylation of IGF-1R induced by its extracellular ligand insulin-like growth factor-1 caused the receptor to bind with IRS-1 10 times faster than the unactivated receptor. As a result, the affinity constants of IRS-1 to phosphorylated and unphosphorylated IGF-1R were (8.06 ± 5.18) × 109M-1and (9.81 ± 4.61) × 108M-1, respectively. on behalf of the Federation of European Biochemical Societies.
Original languageEnglish
Pages (from-to)31-36
Number of pages6
JournalFEBS Letters
Issue number1
Publication statusPublished - 7 Sep 2001


  • Biosensor
  • Insulin receptor substrate-1
  • Insulin-like growth factor-1 receptor
  • Surface plasmon resonance
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this