Spectroscopic, thermodynamic and molecular docking studies of bovine serum albumin interaction with ascorbyl palmitate food additive

摘要

Introduction Ascorbyl palmitate (AP) is an example of natural secondary food antioxidant, which has been used for oxidative rancidity prevention in food industry. In this study, the interaction of AP with bovine serum albumin (BSA) was investigated. Methods The mechanism of BSA interaction with AP was investigated using spectroscopic methods (UV-Vis, fluorescence). The thermodynamic parameters including enthalpy change (??H), entropy change (??S), and Gibba??s free energy (??G) were calculated using Vana??t Hoff equation at different temperatures. Results The experimental results showed that UV-Vis absorption spectra of BSA decreased upon increasing AP concentration, indicating that the AP can bind to BSA. Formation of the AP-BSA complex was approved by quenching of fluorescence and the quenching mechanism was found to be resultant from dynamic procedure. The positive values of both ??H and ??S showed that hydrophobic forces were the major binding forces. The negative value of ??G demonstrated that AP interacts with BSA spontaneously. Molecular docking results confirmed that AP binds to BSA through hydrophobic forces. Conclusion The attained results showed that AP can bind to BSA and effectively distributed into the bloodstream.