Abstract
One of the critical intracellular signal transduction pathway involves the binding of Grb2 SH2 domain to the phosphotyrosine (pTyr) motifs on growth factors such as EGFR and erbB2, leading to downstream activation of the oncogenic Ras signaling pathway. Therefore, the Grb2 SH2 domain has been chosen as our target for development of potential anti-cancer agents. Previously, we reported a series of potent peptides and the detection of their inhibitory effects on the Grb2-SH2 domain. We report here our recent experimental design for detecting the interaction between Grb2-SH2 domain and its ligands using surface plasmon resonance (SPR) technology. Binding interactions between peptides and the Grb2-SH2 domain were measured and analyzed using BIACORE X instrument, which provide detailed information of the real-time detection of the binding interaction. We also established an SPR-based assay to determine the inhibitory effects of a series of designed peptide analogs, and discovered some potent antagonists of the Grb2 SH2 domain. Results of this study should provide important information for further development of peptide or peptidomimetics with high affinity for the Grb2 SH2 domain.
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