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    Elucidating the Interaction Mechanism of Folic Acid with Ovalbumin by Multispectroscopic and Molecular Simulation Methods

    Year: 2021

    Journal: ACS Food Sci. Technol., Volume 1, MAY 21, page 660–668

    Authors: Wang, Junyi; Dadmohammadi, Younas; Jaiswal, Archana; Abbaspourrad, Alireza

    Keywords: ovalbumin; folic acid; thermodynamic parameters; protein structure; solubility; QCM-D

    Pharmaceutical and food applications of folic acid are restrained by its stability and solubility. Different techniques, such as complexation or encapsulation, have been reported to improve stability and solubility. Thus, the understanding of folic acid interaction mechanism with macromolecules like ovalbumin (OVA) is a crucial step. This study characterized the folic acid-OVA interactions using fluorescence titration, FTIR, circular dichroism (CD), quartz-crystal microbalance with dissipation (QCM-D), and molecular docking. Fluorescence titration showed that folic acid could strongly quench the intrinsic fluorescence of OVA through static quenching. The thermodynamic parameters, Delta H (-35.06 kJ mol(-1)), Delta S (-32.27 J mol(-1) K-1 at 298 K), and Delta G (-27.98 kJ mol(-1) at 298 K), revealed that the folic acid-OVA interaction was mainly driven by hydrogen bonding. Molecular docking and QCM-D indicated folic acid could be inserted into the OVA hydrophobic cavity between alpha-helical and beta-sheet-rich domains. This altered OVA conformation by reducing alpha-helix and increasing beta-sheets, proved by CD and FTIR. Furthermore, when the OVA was used as a carrier, the solubility of folic acid increased by 15-fold to 84.05 mu g/mL compared to that of free folic acid.
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