Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 109, Issue -, Pages 1-11Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2011.12.010
Keywords
Chlorpyrifos; Serum albumin; Fluorescence quenching; Circular dichroism; Electrochemistry; FRET
Categories
Funding
- National Natural Science Foundation of China [20921062, 21077081, 21173026]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT1030]
- Natural Science Foundation of Hubei province [2010CDB01302]
- Fundamental Research Funds for the Central Universities of China
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Chlorpyrifos (CPF) is a widely used organophosphate insecticide which could bind with human serum albumin (HSA) and bovine serum albumin (BSA). The binding behavior was studied employing fluorescence, three-dimensional fluorescence, Circular dichroism (CD) spectroscopy, UV-vis absorption spectroscopy, electrochemistry and molecular modeling methods. The fluorescence spectra revealed that CPF causes the quenching of the fluorescence emission of serum albumin. Stern-Volmer plots were made and quenching constants were thus obtained. The results suggested the formation of the complexes of CPF with serum albumins, which were in good agreement with the results from electrochemical experiments. Association constants at 25 degrees C were 3.039 x 10(5) mol L-1 for HSA, and 0.3307 x 10(5) mol L-1 for BSA, which could affect the distribution, metabolism, and excretion of pesticide. The alterations of protein secondary structure in the presence of CPF were confirmed by the evidences from UV and CD spectra. Site competitive experiments also suggested that the primary binding site for CPF on serum albumin is close to tryptophan residues 214 of HSA and 212 of BSA, which was further confirmed by molecular modeling. (C) 2012 Elsevier B.V. All rights reserved.
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