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
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