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Pharmacology

Structure-based design for selective inhibition lowers toxicity

Nature Reviews Clinical Oncology volume 10, page 68 (2013)Cite this article

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A compound that inhibits the growth of BCL-2–dependent tumours has been re-engineered to prevent the concurrent inhibition of the BCL-XL protein that protects platelets, report Andrew Souers and colleagues in Nature Medicine.

Apoptosis is tightly controlled by pro-death and pro-survival proteins. Shifting the balance towards pro-survival proteins is one mechanism by which cancer cells are able to evade apoptosis. BCL-2 is a protein regulator of apoptosis that has a major role in the survival of a number of lymphoid malignancies. BCL-XL is a related pro-survival protein that is associated with a number of haematological malignancies and solid–tumours, and is also is the primary pro-survival factor in platelets.

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ORIGINAL RESEARCH PAPER

  1. Souers, A. J. et al. ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets Nat. Med. doi:10.1038/nm.3048

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  1. Bryony Jones
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Jones, B. Structure-based design for selective inhibition lowers toxicity. Nat Rev Clin Oncol 10, 68 (2013). https://doi.org/10.1038/nrclinonc.2013.1

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