Bitter taste receptors (T2Rs) perform crucial role in the sensation of bitterness, especially the T2R14 that can widely perceive the bitterness. In this study, egg protein-derived T2R14 blocking peptides were identified using physicochemical property prediction, molecular docking, molecular dynamic simulation, and in vitro validation. The ‘-CDOCKER_ENERGY’ values of peptides CQR and CGSR were higher than the positive control LEGSLE, were 314.26 and 294.85 kJ/mol, respectively. The results showed that the half inhibitory concentration (IC50) of the egg protein-derived peptides CQR and CGSR were 382.87 and 370.13 μmol/L, respectively, and higher than that of the positive control LEGSLE. The molecular docking results showed that the conventional hydrogen bond interaction was the main binding force between T2R14 and peptides (i.e., CQR and CGSR). In summary, the novel T2R14 blocking peptides CQR and CGSR were identified, and aided in understanding the mechanism responsible for T2R14 blocking peptides. This study provides further guidance to block T2R14 and may address the bitterness problem in the food industry.