Exploring Interaction Pattern of Benzoic Acid as an Aromatic Ligand With Soy Protein Isolate by Experimental Analysis and Validation by Molecular Docking

ABSTRACT This study aimed to explore benzoic acid (BA) as a ligand for interaction with soy protein isolate (SPI) by molecular docking. First, BA‐incorporated SPI films were prepared by the solution casting method with different contents of BA (1% to 5% w.r.t. 7% SPI) followed by structural characterization by FTIR spectroscopy. FTIR results showed change in the intensity of the peaks at around 802 and 1540 cm −1 . X‐ray diffraction analysis showed that BA‐incorporated SPI films primarily have an amorphous structure with no observable crystalline peaks of BA. From the material properties data, it can be concluded that 2% BA content is optimum for uniform dispersion. Thermal analysis revealed improved stability at lower BA concentration and transmittance studies of the films indicated better optical clarity and UV‐resistance. In silico docking analysis was carried out by BIOVIA Discovery Studio Client to evaluate the roles of covalent and non‐covalent forces acting between BA and SPI. Additionally, CB‐Dock2 was used to predict the 3D structure of a protein and a ligand and also to validate the docking results. Molecular dynamics simulation over 100 ns further validated the docking findings, with Hit_C3 identified as the most stable binding complex based on RMSD, RMSF, and SASA analysis.