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Conformation-Selective Analogues of Dasatinib Reveal Insight into Kinase Inhibitor Binding and Selectivity

  • Frank E. Kwarcinski
  • , Kristoffer R. Brandvold
  • , Sameer Phadke
  • , Omar M. Beleh
  • , Taylor K. Johnson
  • , Jennifer L. Meagher
  • , Markus A. Seeliger
  • , Jeanne A. Stuckey
  • , Matthew B. Soellner
  • University of Michigan, Ann Arbor

Research output: Contribution to journalArticlepeer-review

64 Scopus citations

Abstract

In the kinase field, there are many widely held tenets about conformation-selective inhibitors that have yet to be validated using controlled experiments. We have designed, synthesized, and characterized a series of kinase inhibitor analogues of dasatinib, an FDA-approved kinase inhibitor that binds the active conformation. This inhibitor series includes two Type II inhibitors that bind the DFG-out inactive conformation and two inhibitors that bind the αC-helix-out inactive conformation. Using this series of compounds, we analyze the impact that conformation-selective inhibitors have on target binding and kinome-wide selectivity.

Original languageEnglish
Pages (from-to)1296-1304
Number of pages9
JournalACS Chemical Biology
Volume11
Issue number5
DOIs
StatePublished - May 20 2016

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