<p>CD47, a cell surface protein, serves as a "don't eat me" signal that prevents immune cells from engulfing healthy cells upon its interaction with SIRPα. Cancer cells exploit this mechanism by overexpressing CD47 to evade immune destruction. Blocking the interaction between CD47 and its receptor, SIRPα, is a promising therapeutic strategy. Targeting the interactions between these surface proteins with small molecules is quite challenging, and on the other hand, antibodies offer potential. However, the interactions between antigen (CD47) and antibody (B6H12.2) play a crucial role in this scenario, and increasing the affinity by mutating the interacting residues might impact the inclination and effectiveness of the antibody towards antigen. Thus, this study focuses on designing antibodies with increased affinity and stability towards the antigen compared to the wild-type. Residual scanning calculations were performed to mutate the interacting as well as the hydrophobic residues of the antibody and affinity was assessed. Computational approaches, including antigen-antibody docking studies and molecular dynamics simulations, were employed to evaluate the affinity, stability and therapeutic potential of these modified antibodies.</p>