Survivin, a member of the inhibitor of apoptosis (IAP) proteins family which is up regulated in the majority of cancers, while it is not or transiently expressed in normal and differentiated tissues [1]. Survivin inhibits the process of apoptosis in cancer cells through binding to different apoptotic proteins and inhibiting the activity of caspase-3, caspase-7 and caspase-9[2], as well as enhancing proliferation and induction of chemotherapy resistance. Survivin is regarded as one of the promising anti-cancer drug and cancer-immunotherapy targets. Hitherto several anti-survivin drugs have been developed that have focused on inhibiting survivin expression or surviving mRNA degrading agents. Peptide therapies have only recently being advanced e.g. shepherdin a 9-residue peptide that binds to heat shock protein-90, blocking its interaction with survivin, which in turn results in apoptosis [3]. Current therapies have targeted binding partners of survivin, here we have expressed native survivin and the more active phosphorylated survivin and investigated a series of peptide and structural peptides in binding to survivin and blocking its interaction with apoptotic inducing proteins. The objective of the study is to show that survivin-binding peptides are able to block survivin’s ability to bind to apoptotic inducing proteins and so initiating apoptosis in cancer cells.