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BAM 7 is a direct and selective activator of proapoptotic Bax with IC50 of 3.3 μM.

bam7 is a direct and selective activator of bax with ic50 value of 3.3um [1].in the competitive fluorescence polarization assay (fpa), bam7 competes with fitc–bim sahb for bax binding site(bh3) in a dose dependent manner. bam7 shows no antiapoptotic or bakδc competitive binding interactions even at 50 μm dosing, revealing a remarkable selectivity of bam7 for bax. the interaction between bam7 and bax at the very surface induces the characteristic structural changes that yield functional bax oligomerization. in the in vitro assay, bam7 induces bax-dependent cell death but not the cells with bak. bam7 could be developed to a new generation of apoptotic modulators that directly activate bcl-2 family executioner proteins in cancerand other diseases driven by pathologic apoptotic blockades [1].

BAM7 is a selective activator of BAX, a proapoptotic member of the BCL-2 protein family. BAM7 binds directly to the BAX trigger site, a distinct BH3 binding site that regulates BAX activation, inducing BAX oligomerization, which enables the release of apoptogenic factors that result in cell death. BAM7 is selective for this previously unknown BH3-binding groove on the N-terminal face of BAX.

Bax: 3.3 μM (IC₅₀)

[1] evripidis gavathiotis, denis e reyna, joseph a bellairs, elizaveta s leshchiner, and loren d walensky. direct and selective small-molecule activation of proapoptotic bax. nat chem biol. 2012 july ; 8(7): 639–645.