Native-like mitochondrial membrane mimics for apoptosis-regulating proteins

Mitochondrial apoptosis is a programmed suicide mechanism in cells essential for life. Upon oxidative stress, the mitochondrial outer membrane (MOM) undergoes permeabilization, followed by the release of apoptotic factors. This process is tightly regulated by the Bcl-2 protein family at the MOM. In healthy cells, pro-apoptitic Bax is neutralized by the anti-apoptotic Bcl-2, but any imbalance in this interaction can cause disorders including cancer. The MOM contains several phospholipid classes, including the mitochondria-specific cardiolipin, and a broad distribution of fatty acyl chains. We are using neutron reflectometry to elucidate the function of the Bcl-2 protein family and in this experiment we will recreate the MOM lipid composition from purified yeast lipid extracts to investigate the binding of Bax to native-like MOM mimics.