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Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

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Abstract:

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

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Periodical:

Advanced Materials Research (Volumes 726-731)

Pages:

199-203

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.726-731.199

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Online since:

August 2013

Authors:

Rui Xin Guo*, Zhi Liang Wang, Zhi Jun Hu, Guo Ling Li, Jian Qiu Chen

Keywords:

Bovine Serum Albumin (BSA), Fluorescence Spectrum, Imidacloprid, Thermodynamic Parameters, UV-Vis Absorption Spectrum

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© 2013 Trans Tech Publications Ltd. All Rights Reserved

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References

[1] S. Chiron, A. Fernandez-Alba and A. Rodriguez: Water Res.Vol. 34 (2000), p.366.

Google Scholar

[2] F.J. Byrne, N.C. Toscano: Biol. Control. Vol. 43 (2007), p.130.

Google Scholar

[3] T. Tišler, A. Jemec, B. Mozetic, P. Trebše: Chemosphere Vol. 76 (2009), p.907.

Google Scholar

[4] S.M.T. Shaikh, J. Seetharamappa, P.B. Kandagal, D.H. Manjunatha, S. Ashoka: Dyes and Pigments. Vol. 73 (2007), p.211.

DOI: 10.1016/j.dyepig.2005.11.008

Google Scholar

[5] X.P. Liu, Y.X. Du, W. Sun, J.P. Kou, B.Y. Yu: Spectrochimica Acta PartA. Vol. 74 (2009), p.1189.

Google Scholar

[6] W. Sun, Y.X. Du, J.Q. Chen, J.P. Kou, B.Y. Yu: J.Lumin. Vol. 129 (2009), p.778.

Google Scholar

[7] D.P. Ross, S. Subramanian: J. Biochem. Vol. 20 (1981), p.3096.

Google Scholar

[8] F. Wang, J. Yang, X. Wu, X. Wang, L. Feng, Z. Jia, C. Guo: Adv. Colloid Interface Sci. Vol. 298 (2006), p.757.

Google Scholar

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