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

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.

Systematic investigation of the toxic mechanism of PFOA and PFOS on bovine serum albumin by spectroscopic and molecular modeling.

Perfluorinated compounds (PFCs), an emerging class of globally environmental contaminations, pose a great threat to humans with wide exposure from food and other potential sources. The effects of perfluorooctane sulfonate (PFOS) and perfluorooctanoic acid (PFOA) on bovine serum albumin (BSA) under normal physiological conditions were characterized by fluorescence, UV-Vis absorption, Fourier transform infrared (FT-IR) spectroscopy and molecular docking methods. The fluorescence study suggested that the fluorescence quenching of BSA by PFCs was a static procedure forming a PFCs-BSA complex.

Potential toxicity of amphenicol antibiotic: binding of chloramphenicol to human serum albumin.

Antibiotics are widely used in daily life but their abuse has posed a potential threat to human health. To evaluate the toxicity of chloramphenicol (CAP) at the protein level, the interaction between CAP and human serum albumin (HSA) was investigated by fluorescence, Ultraviolet-visible (UV-Vis) absorption, Fourier transform infrared (FT-IR) spectroscopy and molecular docking methods. Fluorescence data revealed that the fluorescence quenching of HSA by CAP was the result of the formation of CAP-HSA complex, and the binding constant was determined to be 3.