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 SO

SUBMITTER: Wen-Tao CHEN 

PROVIDER: S-EPMC10826827 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature