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Structure-based design, synthesis and biochemical testing of novel and potent Smac peptido-mimetics

  1. Author:
    Sun, H. Y.
    Nikolovska-Coleska, Z.
    Chen, J. Y.
    Yang, C. Y.
    Tomita, Y.
    Pan, H. G.
    Yoshioka, Y.
    Krajewski, K.
    Roller, P. P.
    Wang, S. M.

  2. Author Address

    Univ Michigan, Ctr Comprehens Canc, Dept Internal Med, Ann Arbor, MI 48109 USA. Univ Michigan, Ctr Comprehens Canc, Dept Med Chem, Ann Arbor, MI 48109 USA. Georgetown Univ, Med Ctr, Vincent T Lombardi Canc Res Ctr, Washington, DC 20057 USA. NCI, Frederick Canc Res & Dev Ctr, Med Chem Lab, Frederick, MD 21702 USA Wang, SM, Univ Michigan, Ctr Comprehens Canc, Dept Internal Med, 1500 E Med Ctr Dr, Ann Arbor, MI 48109 USA
    1. Year: 2005
    2. Date: FEB 1
  2. Journal: Bioorganic & Medicinal Chemistry Letters
    1. 15
    2. 3
    3. Pages: 793-797
  4. Type of Article: Article
  1. Abstract:

    Structure-based design, chemical synthesis and biochemical testing of a series of novel Smac peptido-mimetics as inhibitors of XIAP protein are described. The most potent compound, 6j, has a binding affinity (K-i value) of 24 nM to XIAP BIR3 protein and is 24 times more potent than the native Smac AVPI peptide. Further optimization of these potent Smac mimetics may ultimately lead to the development of a novel class of anticancer drugs for the treatment of human cancer by overcoming apoptosis-resistance of cancer cells through targeting the inhibitor of apoptosis proteins. (C) 2004 Elsevier Ltd. All rights reserved

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External Sources

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  2. DOI: 10.1016/j.bmcl.2004.11.008
  3. View record in Web of Science®
  4. WOS: 000226935700060

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