Molecular interaction of soybean protein and piperine by computational docking analyses

This study investigated the interaction of soybean glycinin (11S) and beta-conglycinin (7S) proteins with piperine (PIP) and compared the differences between them. Molecular docking results showed that PIP bound to 11S and 7S mainly through electrostatic, hydrogen bonding, and hydrophobic interactions to form complexes with desirable microstructures, leading to a decrease in the surface hydrophobicity of 7S/11S protein. In particular, the decrease for 11S protein was more pronounced than that for 7S protein, and the affinity of PIP for 11S protein was higher than that for 7S protein. Molecular dynamics (MD) results showed that the binding of PIP to soybean protein was spontaneous. The addition of PIP could cause different changes in the secondary structure of 7S/11S protein, mainly a decrease in beta-sheet and an increase in unordered coil, leading to the unfolding of soybean protein. This study provides a theoretical reference and research basis for elucidating the interaction mechanism between PIP and soybean protein in food systems, which is conducive to the potential application of soybean protein -PIP binding system in the food field.