Interaction of molecules of the neonicotinoid imidacloprid and its structural analogs with human serum albumin

Autor:	N. V. Kovganko, O. V. Sviridov, T. S. Serchenya, Yu. G. Chernov, E. P. Kiseleva, K. I. Mikhailopulo, T. M. Tsvetkova
Rok vydání:	2008
Předmět:	Chromatography Stereochemistry Neonicotinoid Tryptophan Condensed Matter Physics Human serum albumin Fluorescence spectroscopy Hydrophobic effect chemistry.chemical_compound Residue (chemistry) chemistry Imidacloprid parasitic diseases Pyridine medicine Spectroscopy medicine.drug
Zdroj:	Journal of Applied Spectroscopy. 75:857-863
ISSN:	1573-8647 0021-9037
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f4f3d2d151d52d929b3757b0551fbe50 https://doi.org/10.1007/s10812-009-9120-3 Zobrazit plný text záznamu Plný text ve formátu PDF