Mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin

Abstract

The interaction between benthiavalicarb-isopropyl and human serum albumin was studied by ultraviolet-visible absorption, fluorescence, synchronous fluorescence, three-dimensional fluorescence, circular dichroism spectroscopies and molecular docking. The results revealed that the effect of benthiavalicarb-isopropyl on human serum albumin was static quenching. The number of binding sites, binding constants, and binding distance were obtained. The interaction of benthiavalicarb-isopropyl to human serum albumin was mainly through hydrogen bond and van der Waals force. The conformation of human serum albumin changed slightly. The interaction details were studied by molecular docking method. This study elucidated the mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin.

Keywords:

• Benthiavalicarb-isopropyl
• mechanism
• molecular docking
• human serum albumin
• spectroscopic studies

Additional information

Funding

This work was supported by the Department of Education of Heilongjiang Province under Grant [numbers HDRCCX-201611, KJCXZD201712]; the Project funded by China Postdoctoral Science Foundation under Grant [numbers 2019M651316]; the Natural Science Foundation of Heilongjiang Province under Grant [numbers LH2019C055]; the Heilongjiang University Graduate Innovation Research Fund under Grant [numbers YJSCX2019-197HLJU]; the Heilongjiang Provincial Postdoctoral Science Foundation under Grant [numbers LBH-Z18261]; and the MInistry of Agriculture and Rural Affairs of the People’s Republic of China [numbers 14192195].