BAM38

BAM38 is a potent and selective small molecule activator of the pro-apoptotic protein BAX (Bcl-2-associated X protein). Developed through a collaboration between the Albert Einstein College of Medicine and the Dana-Farber Cancer Institute, BAM38 was identified as a next-generation lead following the discovery of BAM7. It functions by directly binding to the BAX 'trigger site,' an allosteric regulatory site on the N-terminal region of the protein. This binding induces a conformational transformation that converts BAX from an inactive state into a lethal form capable of translocating to the mitochondria and causing mitochondrial outer membrane permeabilization (MOMP). By directly activating BAX, BAM38 can bypass the apoptotic blockade often found in cancer cells that overexpress anti-apoptotic BCL-2 family members. Preclinical studies in acute myeloid leukemia (AML) models have demonstrated that BAM38 induces dose-dependent cell death and synergizes with BCL-2/BCL-XL inhibitors such as ABT-737.

Other names

BAX activator molecule 38