• Title of article

    Study on the Molecular Interaction of Anthocyanin-rich Eggplant Extracts with Bovine α-Lactalbumin

  • Author/Authors

    Mohseni-Shahri, F.S Department of Chemistry - Bandar Abbas Branch - Islamic Azad University, Bandar Abbas, Iran , Moeinpour, F Department of Chemistry - Bandar Abbas Branch - Islamic Azad University, Bandar Abbas, Iran

  • Pages
    10
  • From page
    485
  • To page
    494
  • Abstract
    Nasunin is the main phenol-based constituent of the eggplant peels, which is famous for its multiple advantages such as antioxidant activity. The α-lactalbumin (α-lac) is a milk protein with great nutritional importance due to its necessary amino acids’ contents. Mechanism of the interaction of α-lac with nasunin was followed by the in silico and spectroscopy studies. The results of the fluorescence quenching experiments demonstrated a reduction in the fluorescence intensities due to the bonding with the fluorescence residues. The particle size of the α-lac and nasunin complex was considerably bigger than the native protein. Far ultraviolet circular dichroism outcomes indicated that the second structure of the protein was rearranged in presence of nasunin. Molecular docking pointed out that the hydrogen binding had a significant influence on the constitution of nasunin-α-lac complex. The results suggested that α-lac could be a perfect carrier for nasunin loading for additional uses in nutrition field.
  • Keywords
    Anthocyanins , α-Lactalbumin , Nasunin , Fluorescence spectroscopy , Molecular modeling
  • Journal title
    Physical Chemistry Research
  • Serial Year
    2022
  • Record number

    2732330