Characterizations and molecular docking mechanism of the interactions between peptide FDGDF (Phe-Asp-Gly-Asp-Phe) and SOD enzyme

Abstract

In this study, we investigated the antioxidant properties of dry-cured beef crude peptide (BPH) at different storage periods. The combination characteristics of different concentrations of Phe-Asp-Gly-Asp-Phe (FDGDF) and superoxide dismutase (SOD) at different temperatures were analyzed by ultraviolet–visible spectroscopy, fluorescence spectroscopy, and FT-IR spectroscopy, combined with the detection of a SOD activity detection box. It was found that FDGDF could improve the activity of SOD by changing its secondary structure. Bonds were formed at O32/O40/O52 using quantum chemical simulation calculations, and the Fukui index was higher than that of most atoms, indicating that these atoms were more likely to participate in the reaction. SPR biological force analysis showed that FDGDF and SOD were in a fast binding and dissociation mode. This study revealed the theoretical basis for studying the antioxidant mechanism of dry-cured beef and provided ideas for developing new dry-cured beef products.

Keywords

• Beef crude proteins
• Binding sites
• Molecular docking
• SPR