Bax, a pro-apoptotic member of Bcl-2 family proteins, plays a central role in mitochondria-dependent apoptosis. Bax normally resides in the cytosol in a quiescent state. Bax-inhibiting peptide (BIP) is a membrane permeable peptide comprised of five amino acids designed from the Bax-binding domain of Ku70 [M. Sawada, P. Hayes, S. Matsuyama, Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70, Nat. Cell Biol. 5 (2003) 352-357]. It inhibits Bax-mediated translocation of cytochrome c and suppresses mitochondria-dependent apoptosis. BIP was used in order to elucidate its role in preventing retinal ganglion cell (RGC) death from apoptosis after optic nerve transection (ONT) in adult Wistar rats. RGC survival was significantly higher in animals with intravitreal injection of BIP, when compared with control animals. These findings suggest that BIP prevented RGC apoptosis after ONT prompting the suggestion that Bax plays a central role in RGC apoptosis after ONT.