RESUMO
This study was conducted to explore the interaction between two plant-based antiplasmodial compounds, gartanin and friedelin, and bovine serum albumin (BSA). The objectives aimed to elucidate the binding characteristics, structural changes, and thermodynamic parameters associated with the interaction. Various methods were used including UV-vis, fluorescence, and circular dichroism spectroscopy, supported by molecular docking and molecular dynamics simulation. The results showed a concentration-dependent interaction between the antiplasmodial compounds and BSA, revealing changes in protein conformation and stability. The obtained results showed that the plant products bound with BSA through static quenching with moderate binding affinity (104 M-1) with BSA. Thermodynamic parameters and structural transitions calculated from spectroscopic methods revealed that hydrogen bond and van der Waals forces caused the partial conformational alteration in the secondary structure of BSA as the α-helical content decreased with an increase in ß sheets, random coils, and other structures. Computational analysis provided insights into the binding sites and affinities. The study enhances our understanding of the molecular interactions between BSA protein and antiplamodial compounds obtained from plants, supporting the research of choosing, designing, and optimizing molecules for biomedical applications with a focus on selectively targeting their binding sites.
