Interactions between tetrahydroisoindoline-1,3-dione derivatives and human serum albumin via multiple spectroscopy techniques

October 11, 2018

Title

Interactions between tetrahydroisoindoline-1,3-dione derivatives and human serum albumin via multiple spectroscopy techniques

Author

Meiqing Zhu, Lijun Wang, Hao Zhang, Shisuo Fan, Zhen Wang, Qing X. Li, Yi Wang, Shangzhong Liu

Year

2018

Journal

Environmental Science and Pollution Research

Abstract

Some tetrahydroisoindoline-1,3-dione derivatives (TDDs) possess potent herbicidal activity. To assess possible impacts of TDDs on humans, the interactions between TDDs and human serum albumin (HSA) were evaluated with steady-state and time-resolved fluorescence spectroscopy, synchronous fluorescence spectroscopy, Fourier transform-infrared spectroscopy, and circular dichroism spectroscopy. The thermodynamic data obtained at temperatures of 298, 307, and 316 K indicate that TDDs spontaneously bind to HSA and thus form a TDD-HSA complex. The conformation and secondary structure of HSA are changed, and the intrinsic fluorescence of HSA is statically quenched by TDDs. Moreover, the TDD-HSA complex is formed primarily through electrostatic interactions and has only one binding site on HSA. A competitive ligand-binding assay revealed that site II (subdomain IIIA) displays the greatest affinity for TDDs. In addition, an acute toxicity bioassay showed no zebrafish mortality upon exposure to 4000 μg L−1 of TDDs. This work is helpful for understanding interactions between TDDs and HSA.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Ligand binding, Chemical stability, Biochemistry, Agriculture and environmental