Multi-spectroscopies and molecular simulation insights into the interaction mechanism of bovine serum albumin and syringaldehyde

Abstract

Syringaldehyde (Syr) is a natural product with significant biological activities. This study investigated the interaction mechanism of bovine serum albumin (BSA) and Syr through multi-spectroscopies and molecular simulation. The spectroscopy results indicated the binding mechanism of BSA and Syr was static quenching, and the microenvironment of Trp and Tyr residues had changed. Thermodynamic analysis showed that the hydrogen bond and van der Waals force were the main force during the formation of the BSA-Syr complex. The BSA secondary structure changed, and protein became disordered and aggregated with each other with the adding of Syr. Molecular simulation illustrated the Syr mainly bound Trp 213 and Ser 343 of BSA, and formed stable complexes in vivo. It provides guidance for further obtaining highly active Syr analogs. In conclusion, our research provides a theoretical direction for the practical application of Syr and a proposed framework for improving phenolic compounds utilization.