Isoform selective inhibition of STAT1 or STAT3 homo-dimerization via peptidomimetic probes: structural recognition of STAT SH2 domains

  • Bioorg Med Chem Lett. 2007 Apr 1;17(7):1875-8. doi: 10.1016/j.bmcl.2007.01.077.
Patrick T Gunning  1 ,  William P Katt ,  Matthew Glenn ,  Khandaker Siddiquee ,  Joon S Kim ,  Richard Jove ,  Saïd M Sebti ,  James Turkson ,  Andrew D Hamilton
Affiliations
  • 1. Department of Chemistry, Yale University, New Haven, CT, USA.
PMID: 17336521 DOI: 10.1016/j.bmcl.2007.01.077
Abstract

The identification of constitutively activated STAT (Signal Transducers and Activators of Transcription) proteins in aberrant cell signaling pathways has led to investigations targeting the selective disruption of specific STAT isoforms directly associated with oncogenisis. We have identified, through the design of a library of peptidomimetic inhibitors, agents that selectively disrupt STAT1 or STAT3 homo-dimerization at low micromolar concentrations. ISS840 has 20-fold higher inhibition of STAT1 homo-dimerization (IC(50) value of 31 microM) relative to STAT3 (IC(50) value of 560 microM).

Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-186227
    ISS840
    STAT1 Inhibitor
    target: STAT
    Research Areas: Cancer