BAD Peptides

BAD is a family member of the protein BCL-2 and belongs to the BH3 protein subfamily, which includes other members: BH3 BID, BIKand BLK, HRK, BNIP3 and BIM_L. BAD was originally discovered in a yeast two-hybrid system used to screen for BCL-2 interacting proteins. BAD contains a highly conserved α-helical BH3 domain that is a four-turn amphipathic α-helixs with the sequence: Hy-X-X-X-Hy-X-X-X-Sm-D/E-X-Hy. Through this domain, they form heterodimers with BCL-2 and BCLX_L to promote apoptosis.

BCL-2 family proteins, which contains BAD, is essential for determining whether cells survive or die as a result of apoptosis. Dephosphorylation and activation of BAD occur when cells lack growth factors, BAD attaches to the anti-apoptotic members BCL-2-BCL-X_L and releases the pro-apoptotic proteins BAK and BAX, initiating cell apoptosis. BAD protein levels have been reported to be raised in diseases like myocardial ischemia-reperfusion. BAD has also been related to cancer, with reduced levels of BAD leading to malignant tumors in mouse models. Additional research has demonstrated that BAD causes DNA damage when it binds to the tumor suppressor protein p53 and triggers apoptosis in such cells, thus maintaining cell physiology.