Studies on the Mechanism of Interaction of Congo Red with Lysozyme by Spectroscopic Methods

X.H. Li; X.H. Lu; J.P. Liang; Z.J. Xin; X. Zhou

doi:10.14233/ajchem.2013.14291

Issue

Vol. 25 No. 11 (2013): Vol 25 Issue 11

Issue Published : May 18, 2013

This work is licensed under a Creative Commons Attribution 4.0 International License.

Studies on the Mechanism of Interaction of Congo Red with Lysozyme by Spectroscopic Methods

https://doi.org/10.14233/ajchem.2013.14291

X.H. Li

Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, P.R. China

X.H. Lu

Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, P.R. China

J.P. Liang

Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, P.R. China

Z.J. Xin

Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, P.R. China

X. Zhou

Institute of Modern Physics, Chinese Academy of Sciences, Lanzhou 730000, P.R. China

Corresponding Author(s) : J.P. Liang

lixh@impcas.ac.cn

Asian Journal of Chemistry, Vol. 25 No. 11 (2013): Vol 25 Issue 11
Article Published : June 6, 2013

Abstract

Interaction between Congo red and lysozyme was investigated by spectroscopic methods. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding of Congo red with lysozyme. Various binding parameters have been evaluated. The circular dichroism measurements revealed the conformational changes of lysozyme from a-helix to distorted helix structure thereby indicating the conformational change in lysozyme upon binding. The thermodynamic data showed that hydrophobic interactions playing a major role in Congo red binding to lysozyme.

Keywords

Binding Congo red Lysozyme Fluorescence Circular dichroism

Li, X., Lu, X., Liang, J., Xin, Z., & Zhou, X. (2013). Studies on the Mechanism of Interaction of Congo Red with Lysozyme by Spectroscopic Methods. Asian Journal of Chemistry, 25(11), 6146–6150. https://doi.org/10.14233/ajchem.2013.14291

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References

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References

B.P. Kamat and J. Seetharamappa, Polish J. Chem., 78, 723 (2004).

T.B. Tschopp, H.R. Baumgartner and A. Studer, Thromb. Diath. Haemorrh, 26, 488 (1971).

M. Giger, H.R. Baumgartner and G. Zbin den, Agents Act., 4, 173 (1974).

T.J. Haley, Clin Toxicol., 8, 13 (1975).

X. Zhang and J. Jin, J. Mol. Struc., 882, 96 (2008).

J. Jin and X. Zhang, J. Lumin., 128, 81 (2008).

T.V. Zenser, V.M. Lakshmi and B.B. Davis, Drug. Metab. Dispos., 26, 856 (1998).

A.R. Beaudoin, Proc. Soc. Exp. Biol. Med., 117, 176 (1964).

M. Tubis, W.H. Blahd and R.A. Nordyke, J. Am. Pharm. Assoc., 49, 522 (1960).

C.J. Sheng and H.D. Dian, Lysozyme, Shandong Science and Technology Press, 50 (1982).

E. Pigorsch,A. Elhaddaoui and S. Turrell, J. Mol. Struc., 348, 61 (1995).

X.Z. Feng, Z. Lin, L.J. Yang and C. Wang, Talanta, 47, 1223 (1998).

R.C. Lu, J.X. Xiao, A.N. Cao, L.H. Lai, B.Y. Zhu and G.X. Zhao, Biochim. Biophys. Acta, 1722, 271 (2005).

C.Z. Huang, Y.E. Li and X.D. Liu, Anal. Chim. Acta, 375, 89 (1998).

S. Deepa and A.K. Mishra, J. Pharm. Biom. Anal., 38, 556 (2005).

W.Y. He, Y. Li, C.X. Xue, Z.D. Hu, X.G. Chen and F.L. Sheng, Bioorg. Med. Chem., 13, 1837 (2005).

T.G. Dewey, Plenum Press, New York, pp. 1-41 (1991).

J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Plenum Press, New York, pp. 266-7 (1983).

M.X. Xie, M. Long, Y. Liu, C. Qin and Y.D. Wang, Biochim. Biophys. Acta, 1760, 1184 (2006).

A. Papadopoulou, R.J. Green and R.J. Frazier, J. Agric. Food Chem., 53, 158 (2005).

M.X. Xie, X.Y. Xu and Y.D. Wang, Biochim. Biophys. Acta, 1724, 215 (2005).

P.D. Ross and S. Subramanian, Biochemistry, 20, 3096 (1981).

N. Seedher, B. Singh and P. Sing, Indian J. Pharm. Sci., 61, 3 (2004).

F.L. Cui, J. Fan, J.P. Li and Z.D. Hu, Bioorg. Med. Chem., 12, 151 (2004).

Y.J. Hu, Y. Liu, J.B. Wang, X.H. Xiao and S.S. Qu, J. Pharm. Biomed. Anal., 36, 915 ( 2004).

Issue

Vol. 25 No. 11 (2013): Vol 25 Issue 11

Studies on the Mechanism of Interaction of Congo Red with Lysozyme by Spectroscopic Methods

Corresponding Author(s) : J.P. Liang

Abstract

Keywords

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