Yousef Sohrabi
1,2, Vahid Panahi-Azar
3, Abolfazl Barzegar
4, Jafar Ezzati Nazhad Dolatabadi
5* 
, Parvin Dehghan
1*1 Nutrition Research Center, Department of Food Science and Technology, School of Nutrition, Tabriz University of Medical Sciences, Tabriz, Iran
2 Student Research Committee, Tabriz University of Medical Sciences, Tabriz, Iran
3 Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
4 Research Institute for Fundamental Sciences, University of Tabriz, Tabriz, Iran
5 Research Center for Pharmaceutical Nanotechnology, Faculty of Pharmacy, Tabriz University of Medical Sciences, Tabriz, Iran
Abstract
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 (ΔH), entropy change (ΔS), and Gibb’s free energy (ΔG) were calculated using Van’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 ΔH and ΔS showed that hydrophobic forces were the major binding forces. The negative value of ΔG 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.