Comparison of binding interaction between β-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods.

Evaluation of single and combined effects of cadmium and micro-plastic particles on biochemical and immunological parameters of common carp (Cyprinus carpio)

Spatio-temporal distributions and the ecological and health risks of phthalate esters (PAEs) in the surface water of a large, shallow Chinese lake.

Interaction of cyanidin-3-O-glucoside with three proteins.

The interaction between N-acetyl cysteine (NAC) and bovine serum albumin (BSA) was investigated by UV–vis, fluorescence spectroscopy, and molecular docking methods. Fluorescence study at three different temperatures indicated that the fluorescence intensity of BSA was reduced upon the addition of NAC by the static quenching mechanism. Binding constant (Kb) and the number of binding sites (n) were determined. The binding constant for the interaction of NAC and BSA was in the order of 103 M−1, and the number of binding sites was obtained to be equal to 1. Enthalpy (ΔH), entropy (ΔS), and Gibb's free energy (ΔG) as thermodynamic values were also achieved by van't Hoff equation. Hydrogen bonding and van der Waals force were the major intermolecular forces in the interaction process and it was spontaneous. Finally, the binding mode and the binding sites were clarified using molecular docking which were in good agreement with the results of spectroscopy experiments. © 2015 Wiley Periodicals, Inc. Biopolymers 103: 638–645, 2015.

Spectroscopic and molecular docking studies on the interaction between N-acetyl cysteine and bovine serum albumin.

As endocrine-disrupting chemicals, a few frequently used phthalate plasticizers were banned or restricted for use as additives in food in some countries. The interaction mechanisms between three phthalate plasticizers with human serum albumin (HSA) were studied by fluorescence (quenching, synchronous, and three-dimensional), UV-vis absorption, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopy, in combination with molecular modeling under simulative physiological conditions, respectively. The results obtained from fluorescence quenching data revealed that the plasticizers-HSA interaction altered the conformational strcture of HSA. Meanwhile, the alterations of HSA secondary structure in the presence of phthalate plasticizers were investigated. The binding distances for the plasticizers-HSA system were provided by the efficiency of fluorescence resonance energy transfer. Furthermore, the thermodynamic analysis implied that hydrophobic forces were the main interaction for the plasticizers-HSA system, which agreed well with the results from the molecular modeling study.

Zhi-Jie Shan

Papers

Binding of Phthalate Plasticizers to Human Serum Albumin in Vitro: A Multispectroscopic Approach and Molecular Modeling