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Novel peptide inhibitors for Grb2 SH2 domain and their detection by surface plasmon resonance

  1. Author:
    Lung, F. D. T.
    Tsai, J. Y.
    Wei, S. Y.
    Cheng, J. W.
    Chen, C.
    Li, P.
    Roller, P. P.

  2. Author Address

    China Med Coll, Dept Nutr, Taichung 404, Taiwan China Med Coll, Dept Nutr, Taichung 404, Taiwan Natl Tsing Hua Univ, Dept Life Sci, Div Struct Biol & Biomed Sci, Hsinchu 300, Taiwan Acad Sinica, Inst Biomed Sci, Tokyo 115, Japan NCI, Frederick Canc Res & Dev Ctr, Med Chem Lab, Frederick, MD 21702 USA Lung FDT China Med Coll, Dept Nutr, Taichung 404, Taiwan
    1. Year: 2002
  2. Journal: Journal of Peptide Research
    1. 60
    2. 3
    3. Pages: 143-149
  4. Type of Article: Article
  1. Abstract:

    One of the critical intracellular signal transduction pathways involves the binding of the Grb2 SH2 domain to the phosphotyrosine (pTyr) motifs on growth factor receptors, such as epidermal growth factor receptor (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 the development of potential anticancer agents. As a continuation of our earlier work, herein we report the design and synthesis of new peptide analogs, and their inhibitory effect on the Grb2 SH2 domain using surface plasmon resonance (SPR) technology. These novel agents do not contain phosphotyrosine or phosphotyrosine mimics. Binding interactions between these peptides and the Grb2 SH2 domain were measured and analyzed using a BIAcore X instrument, which provides detailed information on the real-time detection of the binding interaction. The results of this study should provide important information for the further development of peptides or peptidomimetics with high affinity for the Grb2 SH2 domain.

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