Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling |
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Authors: | Katarí na Golianov ,Samuel Havadej,Val ria Verebov ,Jozef Uli
ný ,Be ta Hole
kov ,Jana Stani
ov |
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Affiliation: | 1.Faculty of Science, Pavol Jozef Šafárik University, Jesenná 5, 041 54 Košice, Slovakia; (K.G.); (S.H.); (J.U.);2.University of Veterinary Medicine & Pharmacy, Komenského 73, 041 81 Košice, Slovakia; (V.V.); (B.H.);3.First Faculty of Medicine, Charles University, Kateřinská 1, 121 08 Prague, Czech Republic |
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Abstract: | The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods. |
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Keywords: | epoxiconazole prothioconazole interaction serum albumins molecular modeling |
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