Abstract
Pro-apoptotic BAX is a critical BCL-2 family protein that, following death stimuli, is activated and induces mitochondrial outer membrane permeabilization (MOMP), leads to cell apoptosis. It was previously reported that BAX protein in the presence of tBid activator efficiently bind to MOM and cause permeabilization.
Here we determined the dissociation constant (Kd) for BAX binding in the presence and absence of activator protein and the leakage efficiency caused by studied proteins. The research was conducted on a model system of LUVs with a lipid composition similar to the MOM.
The impact of specific oxidized lipids on binding and leakage was also investigated. Our results provide new information about the specificity of the interaction of BAX protein with the lipid bilayer and the leakage caused.