Pro-survival BCL‑2-family proteins are often over-expressed in tumours and essential for their sustained expansion.1 Moreover, the pro-survival BCL-2 family member BCL‑XL renders malignant tumour cells resistant to diverse anti-cancer therapeutics.2 Hence, enhancing apoptotic responses by inhibiting BCL‑XL is likely to have widespread utility in cancer treatment and, compared to inhibiting multiple pro-survival BCL-2 family members, a BCL‑XL-selective inhibitor would be expected to minimize the toxicity to normal tissues.
The BCL-2 family driven apoptosis occurs through a protein-protein interaction cascade between pro-survival and pro-apoptotic members of the family.3 Targeting these proteins — deemed “undruggable” by many pharmaceutical companies — with small molecules has historically been a considerable challenge.
Here, we describe the discovery (by high throughput screen) of a novel series of small molecules targeting BCL‑XL and their structure-guided development. The optimized compound, WEHI-539, has high affinity (sub-nM) and unprecedented selectivity for BCL‑XL. We show that WEHI-539 potently kills cells by selectively antagonizing the pro-survival activity of BCL‑XL.4 WEHI-539 will be an invaluable in vitro tool for distinguishing the roles of BCL-XL from those of its pro-survival relatives, both in normal cells and crucially in malignant tumor cells, many of which may prove to rely upon BCL‑XL for their sustained growth.