Interaction of molecules of the neonicotinoid imidacloprid and its structural analogs with human serum albumin |
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Authors: | K I Mikhailopulo T S Serchenya E P Kiseleva Yu G Chernov T M Tsvetkova N V Kovganko O V Sviridov |
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Institution: | (1) Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 5/2 ul. Kuprevicha, Minsk, 220141, Belarus |
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Abstract: | We have used fluorescence spectroscopy methods to show that imidacloprid and its structural analogs form complexes with human
serum albumin (HSA). The nature of the spectral changes in the ligand×protein systems and the calculated complexation parameters
suggest that these low molecular weight compounds mainly bind to a specific section of the protein molecule, near the tryptophan
residue in the 214 position of the polypeptide chain. We have found that the association constants are on the order of 104 M−1, and the affinity of the ligands for HSA varies in the series 6-chloronicotinic acid > 6-methoxynicotinic acid = imidacloprid
> the keto analog of imidacloprid. The major contribution to the complexation energy probably comes from hydrophobic interaction
forces with participation of the aromatic pyridine ring of the ligands, while additional enhancement of ligand-protein affinity
can be provided by the nitroimine group of imidacloprid.
Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 75, No. 6, pp. 859–866, November–December, 2008. |
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Keywords: | human serum albumin neonicotinoid imidacloprid quenching of fluorescence ligand-protein binding |
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