Interaction of diuron to human serum albumin: Insights from spectroscopic and molecular docking studies

Abstract

This investigation was undertaken to determine the interaction of diuron with human serum albumin (HSA) was studied by monitoring the spectral behavior of diuron-HSA system. The fluorescence of HSA at 340 nm excited at 230 nm was obviously quenched by diuron due to dynamic collision and the quenching constant was of the order of 10(4) L mol(-1) at 310 K. However, no fluorescence quenching was observed when excited at 280 nm. Thermodynamic investigations revealed that the combination between diuron and HSA was entropy driven by predominantly hydrophobic interactions. The binding of diuron induced the drastic reduction in α-helix conformation and the significant enhancement in β-turn conformation of HSA. In addition, both sites marker competition study and molecular modeling simulation evidenced the binding of diuron to HSA primarily took place in subdomain IIIA (Sudlow's site II).

Albumin binding, anticancer and antibacterial properties of synthesized zero valent iron nanoparticles

“…37 Dynamic and static quenching can be distinguished by their different relations on temperature and viscosity. 38 The probability of fluorescence quenching with ligands depends on the rate of collision of the quencher and the ground-state fluorophore (static quenching) or excited fluorophore (dynamic quenching). 39 As shown in Figure 2, the fluorescence intensity of HSA decreases as the ZVFe NP concentration increases at 298 K (Figure 2A), 310 K ( Figure 2B), and 315 K ( Figure 2C).…”