Advancing Scientific Communication about Cancer Research: How to Develop Inhibitors for PD-1 and PD-L1 and Why It Is So Important

Abstract

Cancer cells can gain immunosuppressive functions to avoid being detected by immune cells by turning off certain receptors. PD-1, a checkpoint protein on the surface of T-cells, is deactivated when binding to PD-L1 receptors on the surface of cancer cells. As a result, T cells will not react to cancer cells and the cancer cells will be able to multiply. Our research goal is to create a peptide inhibitor that either binds to PD-1 or PD-L1, allowing the immune system to attack the cancer cells without additional treatments. We focused on optimizing a pull-down assay for detecting the interaction between PD-1 and PD-L1. If successful, this will generate a simple system in which to study peptide inhibitors that bind to PD-1 or PD-L1. However, the two proteins have not been detected to form a complex with each other in the pull-down assays. Another second method used for detecting protein-protein interactions is blue native page gel (BN-PAGE), which can be used to isolate a protein complex based on its size without denaturing the protein in the process. Further research will focus on optimizing both the BN-PAGE as well as the pull-down through buffer screening to ensure that the two proteins can be detected in a complexed state, which is important for downstream inhibitor development.