Inhibitor of MYC identified in a Kröhnke pyridine library

  • Proc Natl Acad Sci U S A. 2014 Aug 26;111(34):12556-61. doi: 10.1073/pnas.1319488111.
Jonathan R Hart  1 Amanda L Garner  2 Jing Yu  2 Yoshihiro Ito  1 Minghao Sun  1 Lynn Ueno  1 Jin-Kyu Rhee  2 Michael M Baksh  2 Eduard Stefan  3 Markus Hartl  3 Klaus Bister  3 Peter K Vogt  4 Kim D Janda  5
Affiliations
  • 1. Departments of Molecular and Experimental Medicine and.
  • 2. Chemistry, The Scripps Research Institute, La Jolla, CA 92037; and.
  • 3. Institute of Biochemistry, University of Innsbruck, 6020 Innsbruck, Austria.
  • 4. Departments of Molecular and Experimental Medicine and [email protected] [email protected].
  • 5. Chemistry, The Scripps Research Institute, La Jolla, CA 92037; and [email protected] [email protected].
Abstract

In a fluorescence polarization screen for the MYC-MAX interaction, we have identified a novel small-molecule inhibitor of MYC, KJ-Pyr-9, from a Kröhnke pyridine library. The Kd of KJ-Pyr-9 for MYC in vitro is 6.5 ± 1.0 nM, as determined by backscattering interferometry; KJ-Pyr-9 also interferes with MYC-MAX complex formation in the cell, as shown in a protein fragment complementation assay. KJ-Pyr-9 specifically inhibits MYC-induced oncogenic transformation in cell culture; it has no or only weak effects on the oncogenic activity of several unrelated oncoproteins. KJ-Pyr-9 preferentially interferes with the proliferation of MYC-overexpressing human and avian cells and specifically reduces the MYC-driven transcriptional signature. In vivo, KJ-Pyr-9 effectively blocks the growth of a xenotransplant of MYC-amplified human Cancer cells.

Keywords
combinatorial library; gene signature; protein–protein interactions; transcriptional control; xenograft.
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