Survivin, a member of the inhibitor of apoptosis (IAP) proteins family, 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 survivin mRNA degrading agents. Peptide therapies have only recently been demonstrated 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 including caspases. However, there is no structural information available on how survivin inhibits caspases to guide structure-based drug design. To address this, we investigated the interaction of recombinantly produced survivin and survivin peptides with several members of the caspase family in search for caspase inhibiting peptides. From an overlapping surviving-derivived peptide library, peptides that bound to and inhibited caspase-9 activity were identified. To further understand the mechanism of action of these peptides and to increase the affinity and efficacys we applied structural studies and alanine scanning on the inhibiting peptides. We expect that our work will shed light into the mechanisms of survivin action on caspases and provide avenues for development of caspase inhibitors.