Flupyrimin and nitenpyram are emerging neonicotinoid insecticides that may cause potential harm to the human body. In the present work, the interactions of flupyrimin/nitenpyram with serum albumins under normal physiological conditions were thoroughly studied by using multiple spectroscopic techniques, DFT calculations and molecular docking. Flupyrimin/nitenpyram can quench the endogenous fluorescence of HSA/BSA and form a complex with HSA/BSA through a static process, causing conformational and secondary structure changes of HSA/BSA. Thermodynamic analysis shows that the combination of flupyrimin/nitenpyram with HSA/BSA is a spontaneous process, mainly driven by hydrogen bonds and hydrophobic forces. Site marking and molecular docking experiments indicated that flupyrimin/nitenpyram binds with HSA/BSA at site II (subdomain IIIA). The binding constant Ka in HSA-flupyrimin, HSA-nitenpyram, BSA-flupyrimin and BSA-nitenpyram systems at 298 K was 2.11 × 105 M-1, 2.35 × 105 M-1, 1.91 × 105 M-1 and 2.11 × 105 M-1, respectively. The binding constant Ka of nitenpyram with HSA/BSA was greater than flupyrimin, indicating that nitenpyram binds HSA/BSA was more stable than that of flupyrimin, which was consistent with the DFT calculation. In addition, the acute toxicity bioassay showed that flupyrimin and nitenpyram exhibited low toxicity to zebrafish, with 96 h LC50 values of 181.662 and 250.658 mg a. i. L-1, respectively. These results can help understand the interactions of flupyrimin/nitenpyram with HSA/BSA.
Keywords: Albumin; Fluorescence spectroscopy; Molecular modeling; Neonicotinoid insecticides.
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