Molecular and technical aspects on the interaction of bovine serum albumin with pyrazine derivatives: From molecular docking to spectroscopy study

In order to better understand the transport and action mechanism of flavor substance and proteins in human body, the interaction mechanism between pyrazine derivatives and bovine serum albumin (BSA) was studied by molecular dynamics simulation and a series of spectroscopic methods. In molecular docking, it was observed that the small molecules were surrounded by hydrophobic amino acid residues of the protein, and the main amino acid residues formed π-π interaction and hydrogen bond interaction with BSA. The results of fluorescence emission spectroscopy combined with thermodynamic analysis showed that static quenching was the main mechanism of the interaction between three pyrazine derivatives and BSA, which was dominated by hydrophobic interaction. Synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy combined with molecular dynamics simulation proved that the pyrazine derivatives changed the conformation of BSA. In summary, pyrazine derivatives can interact with BSA, and the complexation of the complex changes its spatial conformation. The research in this paper has positive significance for understanding the binding, transport, and metabolism of pyrazine compounds in the process of blood circulation and provides key data for the metabolism of pyrazine compounds in vivo. PRACTICAL APPLICATION: The interaction of pyrazine derivatives-BSA is studied by multi-spectra and MD. The fluorescence quenching of pyrazine derivatives-BSA is static quenching. The main force between pyrazine derivatives and BSA is hydrophobic force. There is only one site of association between pyrazine derivatives and BSA. Pyrazine derivatives have effects on conformation of BSA.