作者: Ana J. García-Sáez , Salvatore Chiantia , Jesús Salgado , Petra Schwille
DOI: 10.1529/BIOPHYSJ.106.100370
关键词: Peptide binding 、 Cell biology 、 Bcl-2-associated X protein 、 Protein structure 、 Membrane 、 Membrane fluidity 、 Lipid bilayer 、 Liposome 、 Peptide 、 Chemistry
摘要: Bax is a critical regulator of physiological cell death that increases the permeability outer mitochondrial membrane and facilitates release so-called apoptotic factors during apoptosis. The molecular mechanism action unknown, but it probably involves formation partially lipidic pores induced by Bax. To investigate interaction with lipid membranes physical changes underlying pores, we used an active peptide derived from helix 5 this protein (Bax-α5) able to induce Bax-like in bilayers. We report decrease line tension due binding both at domain interface phase-separated bilayers pore edge atomic force microscopy film-rupture experiments. Such may be general strategy pore-forming peptides proteins, as affects energetics stabilizes open state.