Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 94, Issue 3, Pages 158-163Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2008.10.001
Keywords
Thiophanate methyl (MT); Human serum albumin; Fluorescence quenching technique; FT-IR spectroscopy; Molecular modeling
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Thiophanate methyl (MT) is one of the widely used fungicides to control important fungal diseases of crops, which has led to potential toxicological risk to public health. Several different transport proteins exist in blood plasma, but albumin only is bound by a wide diversity of xenobiotics reversibly with high affinity. We studied the interaction of MT with human serum albumin by using spectroscopic methods including fluorescence quenching technology, UV and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The result of fluorescence titration revealed that MT could quench the intrinsic fluorescence of HSA. The binding process was exothermic and spontaneous, as indicated by the thermodynamic analyses. In addition, the studies of FT-IR spectroscopy showed that the binding of MT to HSA changed molecular conformation of HSA. The results obtained from molecular modeling showed that the interaction between NIT and HSA was dominated by hydrophobic force, and there was also hydrogen bond interaction between the pesticide and the residues of HSA, which was in good agreement with the result of binding mode. (C) 2008 Elsevier B.V. All rights reserved.
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