Evaluation of natamycin interaction with serum albumin protein using spectroscopic methods and surface plasmon resonance (SPR)

Abstract

Conclusions: In the current study, the interaction between NT and BSA was explored using different spectroscopic techniques, SPR techniques, and molecular docking modeling. The results of fluorimetry measurements showed that NT reduces the intensity of BSA fluorescence by forming a complex with BSA through a hybrid quenching mechanism. Negative values of both ΔH° and ΔS° confirm that van der Waals forces or hydrogen bonds are the basic forces in the interaction of NT with BSA. The negative ΔG value confirmed the spontaneous binding of this ligand onto BSA without any requirement for external energy. The results of the blind docking at molecular docking study displayed that NT could bind to a pit that is located among IIIA (Sudlow I) and IB domains. In addition, Ser 109, Asp111, Lys114, Leu115, Glu424, and Arg 458 also play important roles in NT-BSA interaction.

Keywords: Natamycin; serum albumin; spectroscopic technique; surface plasmon resonance; docking simulation.