Abstract
Imidacloprid belongs to a major new class of insecticides, called neonicotinoids, which are accounting for 11–15% of the total insecticide market. The binding characteristics of insecticide imidacloprid with hemoglobin (Hb) have been studied by employing different spectroscopic techniques. The results proved the formation of complex between imidacloprid and Hb. Hydrophobic interaction and hydrogen bond dominated in the association reaction. Hydrophobic probe 8-anilino-1-naphthalenesulfonic acid (ANS) competitive experiments indicated that the binding of imidacloprid to Hb primarily took place in hydrophobic regions. The distance between Hb donor and acceptor imidacloprid was 4.88 nm as derived from Förster’s theory. Alternations of Hb secondary structure in the presence of imidacloprid were confirmed by synchronous fluorescence, circular dichroism (CD) and three-dimensional fluorescence spectra. This study enriches our understanding of toxic effect of imidacloprid to the physiologically important protein Hb.
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Acknowledgements
The authors are grateful to Professor Yurong Ma of College of Chemistry and Molecular Engineering, Peking University, for her constant support and expert assistance during the CD measurement experiments.
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Ding, F., Han, BY., Liu, W. et al. Interaction of Imidacloprid with Hemoglobin by Fluorescence and Circular Dichroism. J Fluoresc 20, 753–762 (2010). https://doi.org/10.1007/s10895-010-0618-0
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DOI: https://doi.org/10.1007/s10895-010-0618-0