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Updated: Apr 21, 2026

Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells
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Real-Time Monitoring of Aurora kinase A Activation using Conformational FRET Biosensors in Live Cells

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SAR156497, an exquisitely selective inhibitor of aurora kinases

Jean-Christophe Carry1, François Clerc, Hervé Minoux

  • 1Oncology Drug Discovery, ‡Structure Design Informatics, §Disposition Safety Animal Research, ∥Chemical Development, and ⊥Analytical Sciences, Sanofi , 13 Quai Jules Guesde, 94403 Vitry-sur-Seine, France.

Journal of Medicinal Chemistry
|November 5, 2014
PubMed

Insights

Researchers discovered SAR156497, a novel inhibitor targeting Aurora kinases A, B, and C. This selective molecule shows efficacy in vitro and in vivo, offering potential for new cancer therapies.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Oncology

Background:

  • Aurora kinases are critical serine/threonine kinases regulating mitosis.
  • Aberrant Aurora kinase expression is linked to various malignancies.
  • Development of selective Aurora kinase inhibitors is a key area in cancer therapy research.

Purpose of the Study:

  • To discover and optimize novel small molecule inhibitors of Aurora kinases.
  • To identify a selective inhibitor with potential anticancer therapeutic applications.

Main Methods:

  • Discovery and structure-activity relationship (SAR) studies of a novel series of tricyclic molecules.
  • In vitro and in vivo testing of the lead compound for efficacy and selectivity.
  • Co-crystallography or structural analysis to elucidate the binding mode and selectivity.

Main Results:

  • Identification of SAR156497, a potent and selective inhibitor of Aurora A, B, and C kinases.
  • Demonstration of in vitro and in vivo efficacy of SAR156497.
  • Elucidation of the molecular basis for SAR156497's selectivity towards Aurora kinases.

Conclusions:

  • SAR156497 represents a promising novel tricyclic inhibitor targeting Aurora kinases.
  • Its exquisite selectivity and demonstrated efficacy support its potential as an anticancer therapeutic agent.
  • Understanding the binding mode provides valuable insights for future drug design.

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