Triumph at Lorne: Saharnaz Rafiee and Bindusmita Paul Shine in Poster Competition
Congratulations to Saharnaz Rafiee and Bindusmita Paul for their outstanding achievements at the 49th Lorne Protein Conference, where they emerged victorious in the poster competition. Saharnaz presented her groundbreaking research, "Developing innovative survivin-derived peptide inhibitors targeting caspase-9," while Bindusmita showcased her work on "Characterisation of the structure and dynamics of oral polymicrobial biofilms." Their exceptional contributions stood out among approximately 200 poster presentations, reflecting their dedication and excellence at this esteemed international event.
Reflecting on her success, Saharnaz Rafiee shared, "I am delighted to share that I had the honour of winning one of the best poster presentation awards at this year's Lorne Protein Conference. It was a fantastic opportunity to contribute to the scientific discourse and receive recognition for my research efforts."
Abracts
Developing innovative survivin-derived peptide inhibitors targeting caspase-9 Saharnaz Rafiee | 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. Our research focuses on developing innovative survivin-derived peptide inhibitors targeting caspase-9, a key protein involved in apoptosis. Survivin inhibits the process of apoptosis in cancer cells by binding to different apoptotic proteins and inhibiting the activity of caspase-3, caspase-7, and caspase-9. This inhibitory action enhances proliferation and induces chemotherapy resistance in cancer cells. While several anti-survivin drugs have been developed, structural information on how survivin inhibits caspases is lacking. Our study involved investigating the interaction of recombinantly produced survivin and survivin peptides with members of the caspase family to identify peptides that bound to and inhibited caspase-9 activity. Through an overlapping survivin-derived peptide library, we identified peptides that bound to and inhibited caspase-9 activity. Further structural studies and alanine scanning were applied to understand the mechanism of action of these peptides, aiming to increase their affinity and efficacy. We anticipate that our work will provide valuable insights into the mechanisms of survivin action on caspases and open avenues for the development of caspase inhibitors in the fight against cancer. |