Regulation of molecular orientation of charged dipeptides and involved interactions by electrostatic repulsion from like-charged surfaces were studied using all-atom molecular dynamics simulations. It was found that a charged surface can induce oriented alignment of like-charged peptides, and the oriented alignment leads to enhanced electrostatic repulsion between the peptide molecules. The findings are consistent with previous experimental results about the inhibition of charged protein aggregation using like-charged ion-exchange resin. Furthermore, the simulations provided molecular insights into this process, and demonstrated the distinct regulation effect of like-charged surfaces on the molecular interactions between peptides that possess an electric dipole structure. Both the charged surface and the electric dipole structure of peptides were confirmed to be crucial for the regulation. The research is expected to facilitate the rational design of surfaces or devices to regulate the behavior of amphoteric molecules such as proteins for both in vivo and in vitro applications, which would contribute to the regulation of protein-protein interactions and its application in life science and biotechnology.