1. Academic Validation
  2. The allosteric inhibitor ABL001 enables dual targeting of BCR-ABL1

The allosteric inhibitor ABL001 enables dual targeting of BCR-ABL1

  • Nature. 2017 Mar 30;543(7647):733-737. doi: 10.1038/nature21702.
Andrew A Wylie 1 Joseph Schoepfer 2 Wolfgang Jahnke 2 Sandra W Cowan-Jacob 2 Alice Loo 1 Pascal Furet 2 Andreas L Marzinzik 2 Xavier Pelle 2 Jerry Donovan 1 Wenjing Zhu 1 Silvia Buonamici 1 A Quamrul Hassan 1 Franco Lombardo 1 Varsha Iyer 2 Michael Palmer 1 Giuliano Berellini 1 Stephanie Dodd 1 Sanjeev Thohan 1 Hans Bitter 1 Susan Branford 3 David M Ross 4 Timothy P Hughes 5 Lilli Petruzzelli 1 K Gary Vanasse 1 Markus Warmuth 1 Francesco Hofmann 2 Nicholas J Keen 1 William R Sellers 1
Affiliations

Affiliations

  • 1 Novartis Institutes for BioMedical Research, Cambridge, Massachusetts 02139, USA.
  • 2 Novartis Institutes for BioMedical Research, Basel, Switzerland.
  • 3 Centre for Cancer Biology, SA Pathology and University of South Australia, Adelaide, South Australia 5000, Australia.
  • 4 Haematology Directorate, SA Pathology, PO Box 14, Rundle Mall, Adelaide, South Australia 5000, Australia.
  • 5 South Australian Health &Medical Research Institute (SAHMRI), North Terrace, Adelaide, South Australia 5000, Australia.
Abstract

Chronic myeloid leukaemia (CML) is driven by the activity of the BCR-ABL1 fusion oncoprotein. ABL1 kinase inhibitors have improved the clinical outcomes for patients with CML, with over 80% of patients treated with imatinib surviving for more than 10 years. Second-generation ABL1 kinase inhibitors induce more potent molecular responses in both previously untreated and imatinib-resistant patients with CML. Studies in patients with chronic-phase CML have shown that around 50% of patients who achieve and maintain undetectable BCR-ABL1 transcript levels for at least 2 years remain disease-free after the withdrawal of treatment. Here we characterize ABL001 (asciminib), a potent and selective allosteric ABL1 inhibitor that is undergoing clinical development testing in patients with CML and Philadelphia chromosome-positive (Ph+) acute lymphoblastic leukaemia. In contrast to catalytic-site ABL1 kinase inhibitors, ABL001 binds to the myristoyl pocket of ABL1 and induces the formation of an inactive kinase conformation. ABL001 and second-generation catalytic inhibitors have similar cellular potencies but distinct patterns of resistance mutations, with genetic barcoding studies revealing pre-existing clonal populations with no shared resistance between ABL001 and the catalytic inhibitor nilotinib. Consistent with this profile, acquired resistance was observed with single-agent therapy in mice; however, the combination of ABL001 and nilotinib led to complete disease control and eradicated CML xenograft tumours without recurrence after the cessation of treatment.

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