Determination of Binding Potency of Peptidic Inhibitors of Grb2-SH2 by Using the Protein-Captured Biosensor Method

Author(s): Feng-Di T. Lung, Wan-Ching Li, Yung-Hsien Chang, Hui-Ming Chen

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 8 , 2008

Become EABM
Become Reviewer
Call for Editor


The growth factor receptor-binding protein 2 – Src homology 2 (Grb2 – SH2) domain plays an important role in the oncogenic Ras signal transduction pathway, therefore, peptidic inhibitors of the Grb2 – SH2 domain has been chosen as our target for the development of antiproliferative agents. The inhibitory effects of peptide analogs on the Grb2 – SH2 domain have been determined by using surface plasmon resonance (SPR) technology developed with the BIACORE biosensor. Recently, we reported the analysis of interactions between peptides and the GST-Grb2-SH2 that was immobilized on the surface of sensor chip by using BIACORE biosensor (the protein-immobilized method). Herein, we analyze interactions of peptides with the GST-Grb2-SH2 that was captured by the anti-GST antibodies immobilized on the surface of sensor chip (the protein-captured method). Results obtained by both methods are in good correlation, indicating the immobilization of GST-Grb2-SH2 on the sensor chip did not significantly affect the binding of Grb2-SH2 with peptides. Both SPR-based assays are very sensitive bioanalytical methods and can be applied in screening inhibitors of target proteins or purifying GST-fusion proteins, however, considering the efficiency and the cost, the GST-Grb2-SH2-immobilized method is suggested for routinely determining the binding potency of inhibitors of Grb2-SH2.

Keywords: Grb2-SH2, biosensors, surface plasmon resonance, biosensor, BIACORE X, peptide, inhibitor

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2008
Published on: 01 March, 2012
Page: [806 - 810]
Pages: 5
DOI: 10.2174/092986608785203683
Price: $65

Article Metrics

PDF: 2