Journal
SPECTROSCOPY LETTERS
Volume 53, Issue 5, Pages 360-371Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/00387010.2020.1756343
Keywords
Benthiavalicarb-isopropyl; mechanism; molecular docking; human serum albumin; spectroscopic studies
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Funding
- Department of Education of Heilongjiang Province [HDRCCX201611, KJCXZD201712]
- China Postdoctoral Science Foundation [2019M651316]
- Natural Science Foundation of Heilongjiang Province [LH2019C055]
- Heilongjiang University Graduate Innovation Research Fund [YJSCX2019-197HLJU]
- Heilongjiang Provincial Postdoctoral Science Foundation [LBH-Z18261]
- MInistry of Agriculture and Rural Affairs of the People's Republic of China [14192195]
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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.
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