This study investigates the non-covalent interactions between rice protein (RP) and three polyphenols—curcumin (CUR), quercetin (QUE), and resveratrol (RES)—and their potential application as emulsifiers in emulsions. The results show that QUE has the strongest binding affinity with RP, leading to significant structural changes in RP. Molecular docking analysis revealed that hydrophobic interactions, hydrogen bonding, and van der Waals forces drive these interactions. The formation of RP-polyphenol complexes increases the particle size of the complexes and enhances their radical scavenging capacity. Compared to pure RP, the complexes create emulsions with smaller particle sizes (378–395 nm vs. 470 nm), higher zeta potential (37.43–38.26 mV vs. 35.62 mV), and greater lipid oxidation stability. The synergistic effect of polyphenols and protein also improves the antioxidant capacity of the complexes. The study also demonstrates that the structural changes induced by QUE significantly alter the secondary structure of RP, leading to enhanced emulsification performance. The findings suggest that RP-polyphenol complexes can be used as effective emulsifiers in food systems, offering improved stability and functionality.This study investigates the non-covalent interactions between rice protein (RP) and three polyphenols—curcumin (CUR), quercetin (QUE), and resveratrol (RES)—and their potential application as emulsifiers in emulsions. The results show that QUE has the strongest binding affinity with RP, leading to significant structural changes in RP. Molecular docking analysis revealed that hydrophobic interactions, hydrogen bonding, and van der Waals forces drive these interactions. The formation of RP-polyphenol complexes increases the particle size of the complexes and enhances their radical scavenging capacity. Compared to pure RP, the complexes create emulsions with smaller particle sizes (378–395 nm vs. 470 nm), higher zeta potential (37.43–38.26 mV vs. 35.62 mV), and greater lipid oxidation stability. The synergistic effect of polyphenols and protein also improves the antioxidant capacity of the complexes. The study also demonstrates that the structural changes induced by QUE significantly alter the secondary structure of RP, leading to enhanced emulsification performance. The findings suggest that RP-polyphenol complexes can be used as effective emulsifiers in food systems, offering improved stability and functionality.