Molecular interactions between soybean glycinin (11S) and genistein using spectroscopic and in silico analyses

Interactions and binding mechanisms between soybean glycinin (11S) and genistein were investigated at near neutral pH (7.4) and ambient temperature using various spectroscopic techniques and molecular docking. Ultraviolet visible spectroscopy revealed non-covalent bonds were responsible for the stabilisation of the complex. Following complexation, minor reductions in the alpha helix and beta sheet content of the protein were confirmed by circular dichroism (CD) and infrared spectroscopy (FTIR). Fluorescence quenching and molecular docking predicted a 11S trimer and genistein complex with a 1:1 stoichiometric ratio, with the binding location predominantly on the interior portion of the protein, stabilised in majority by hydrogen bonds. Although binding was determined to be of moderate strength, secondary structure characterisation suggested that the structural components of the protein remained largely unchanged. This outcome indicates that the ligand can be accommodated in the interior of the 11S trimer, forming a stable complex within the present conditions of neutral pH and ambient temperature.

Automated summary

The interactions and binding mechanisms between soybean glycinin (11S) and genistein were investigated using spectroscopic techniques and molecular docking. The complex was stabilized by non-covalent bonds. The binding location was predominantly on the interior portion of the protein and was mainly stabilized by hydrogen bonds, forming a stable complex within the present conditions of neutral pH and ambient temperature.