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Development of L-3-aminotyrosine suitably protected for the synthesis of a novel nonphosphorylated hexapeptide with low-nanomolar Grb2-SH2 domain-binding affinity

  1. Author:
    Song, Y. L.
    Roller, P. P.
    Long, Y. Q.

  2. Author Address

    CAS, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China. NCI, Med Chem Lab, NIH, Frederick, MD 21702 USA. Long, YQ, CAS, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, 555 Zuchongzhi Rd, Shanghai 201203, Peoples R China
    1. Year: 2004
  2. Journal: Bioorganic & Medicinal Chemistry Letters
    1. 14
    2. 12
    3. Pages: 3205-3208
  4. Type of Article: Article
  1. Abstract:

    Synthesis of orthogonally protected (2S)-2-amino-3-(3 -amino-4-hydroxy-phenyl)-propionic acid (10) suitable for solid phase peptide synthesis and its first use for the preparation of nonphosphorylated Grb2-SH2 domain antagonists (4a-c) are reported. The 3-aminotyrosine containing sulfoxide-cyclized hexapeptide (4b) exhibited potent Grb2-SH2 domain binding affinity with IC50 = 50 nM which represents the highest affinity yet reported for a peptide inhibitor against Grb2-SH2 domain with only six residues free of phosphotyrosine or phosphotyrosine mimics. This potent small peptidomimetic 4b may be representative of a new class of therapeutically relevant Grb2-SH2 domain-directed agents, and acts as a chemotherapeutic lead for the treatment of erbB2-related cancers. (C) 2004 Elsevier Ltd. All rights reserved

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