Cancer remains a leading cause of death worldwide and arises from genetic and epigenetic alterations that disrupt normal cellular regulation. Immune checkpoint pathways, particularly those involving CTLA-4, play a crucial role in suppressing antitumor immune responses. Immune checkpoint inhibitors such as Tremelimumab have revolutionized cancer therapy by restoring T-cell activity. Improving antibody-receptor interactions through molecular modification may further enhance therapeutic outcomes. Computational approaches such as molecular docking offer valuable tools for studying protein-protein interactions and guiding antibody optimization. The three-dimensional structure of the CTLA-4 receptor was obtained from the Protein Data Bank and prepared through energy minimization. The Tremelimumab antibody was modeled and modified at selected binding regions. Molecular docking simulations were performed to evaluate the interactions between the antibody and receptor. Docking complexes were analyzed for binding affinity, hydrogen bonding, and hydrophobic interactions using molecular visualization tools. Docking results demonstrated stable binding between modified Tremelimumab and CTLA-44. Certain modifications resulted in improved binding affinity, indicated by lower docking energy scores and enhanced interaction networks. Other modifications negatively affected binding due to steric hindrance or loss of key interactions. The study highlights the importance of antibody structure in determining immune checkpoint binding efficiency. Enhanced binding affinity may improve CTLA-4 blockade and strengthen antitumor immune responses. Molecular docking proved effective in predicting interaction patterns, though experimental validation is necessary to confirm biological relevance. This study aims to demonstrate that molecular modification of Tremelimumab can influence its interaction with CTLA-4.