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Received: 2005-08-10

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Journal of Zhejiang University SCIENCE B 2006 Vol.7 No.6 P.452-458


Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin

Author(s):  FAN Ji-cai, CHEN Xiang, WANG Yun, FAN Cheng-ping, SHANG Zhi-cai

Affiliation(s):  Department of Chemistry, Zhejiang University, Hangzhou 310027, China

Corresponding email(s):   shangzc@mail.hz.zj.cn

Key Words:  Pefloxacin mesylate (PFLX), Bovine lactoferrin (BLf), Human serum albumin (HSA), Fluorescence spectra, Energy-transfer efficiency

FAN Ji-cai, CHEN Xiang, WANG Yun, FAN Cheng-ping, SHANG Zhi-cai. Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin[J]. Journal of Zhejiang University Science B, 2006, 7(6): 452-458.

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T1 - Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin
A1 - FAN Ji-cai
A1 - CHEN Xiang
A1 - WANG Yun
A1 - FAN Cheng-ping
A1 - SHANG Zhi-cai
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VL - 7
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PB - Zhejiang University Press & Springer
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DOI - 10.1631/jzus.2006.B0452

The binding of pefloxacin mesylate (PFLX) to bovine lactoferrin (BLf) and human serum albumin (HSA) in dilute aqueous solution was studied using fluorescence spectra and absorbance spectra. The binding constant K and the binding sites n were obtained by fluorescence quenching method. The binding distance r and energy-transfer efficiency E between pefloxacin mesylate and bovine lactoferrin as well as human serum albumin were also obtained according to the mechanism of Förster-type dipole-dipole nonradiative energy-transfer. The effects of pefloxacin mesylate on the conformations of bovine lactoferrin and human serum albumin were also analyzed using synchronous fluorescence spectroscopy.

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article


[1] Aguila, A., Brock, J.H., 2001. Lactoferrin: antimicrobial and diagnostic properties. Biotechnology Apply, 18:76-83.

[2] Baker, E.N., Anderson, B.F., Baker, H.M., MacGillivray, R.T.A., Moore, S.A., Peterson, N.A., Shewry, S.C., Tweedie, J.W., 1998. Three-dimensional structure of lactoferrin—Implications for function, including comparisons with transferring. Advances in Experimental Medicine and Biology, 443:1-14.

[3] Baptista, M.S., Indig, G.L., 1998. Effect of BSA binding on photophysical and photochemical properties of triarylmethane dyes. Journal of Physical Chemistry B, 102(23):4678.

[4] Blandeau, J.M., 1999. Expanded activity and utility of the new fluoroquinolones: a review. Clinical Therapeutics, 21(1):3-40.

[5] Chen, G.Z., Hang, X.Z., Xu, X.Z., Zheng, Z.Z., Wang, Z.B., 1990. Method of Fluorescence Analysis, 2nd Ed. Science Press, Beijing (in Chinese).

[6] Congdon, R.W., Muth, G.W., Splittgerber, A.G., 1993. The binding interaction of Coomassie Blue with proteins. Analytical Biochemistry, 213(2):407.

[7] Fletcher, J.E., Spector, A.A., Ashbrook, J.D., 1970. Analysis of macromolecule-ligand binding by determination of stepwise equilibrium constants. Biochemistry, 9(23):4580.

[8] Horrocks, W.D., Collier, W.E., 1981. Lanthanide ion luminescence probes. Measurement of distance between intrinsic protein fluorophores and bound metal ions: quantitation of energy transfer between tryptophan and terbium (III) or europium (III) in the calcium-binding protein parvalbumin. J. Am. Chem. Soc., 103(10):2856.

[9] Jiang, C.Q., Gao, M.X., He, J.X., 2002. Study of the interaction between terazosin and serum albumin: synchronous fluorescence determination of terazosin. Analytica Chimica Acta, 452(2):185.

[10] Klotz, I.M., Hunstone, D.L., 1971. Properties of graphical representations of multiple classes of binding sites. Biochemistry, 10(16):3065.

[11] Lampreave, F., Pineiro, A., Brock, J.H., Castillo, H., Sanchez, L., Calvo, M., 1990. Interaction of bovine lactoferrin with other proteins of milk whey. International Journal of Biological Macromolecules, 12(1):2.

[12] Ma, C.Q., Li, K.A., Zhao, F.L., Tong, S.Y., 1999. A study on the reaction mechanism between chrome-azurol S and bovine serum albumin. Acta Chimica Sinica, 57(2):389.

[13] Masson, P.L., Heremans, J.F., Dive, J.H., 1966. An iron-binding protein common to many external secretions. Clinica Chimica Acta, 14(6):735.

[14] Masson, P.L., Heremans, J.F., Schonne, E., 1969. Lactoferrin aniron-binding protein in neutrophilic leukocytes. Journal of Experimental Medicine, 130(3):643.

[15] Sanchez, L., Calvo, M., Brock, J.H., 1992. Biological role of lactoferrin. Archives of Disease in Childhood, 67(2):657.

[16] Scatchard, G., 1949. The attractions of proteins for small molecules and ions. Annals of the New York Academy Sciences, 51:660.

[17] Shaklai, N., Yguerabide, J., Ranney, H.M., 1977. Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. Biochemistry, 16(25):5585.

[18] Wang, R.L., Yuan, Z.P., 1999. Handbook of Chemical Products, Drugs. Chemical Industry Press, Beijing, p.166-167 (in Chinese).

[19] Yang, P., Gao, F., 2002. Theory of Bioinorganic Chemistry. Science Press, Beijing, p.331 (in Chinese).

[20] Yang, M.M., Yang, P., Xi, X.L., 1997. Study of the interaction between fluorochrome probe and albumin. Chinese Science Bulletin, 42(12):1276-1279 (in Chinese).

[21] Yuan, T., Weljie, A.M., Vogel, H.J., 1998. Tryptophan fluorescence quenching by methionine and selenomethionine residues of calmodulin: orientation of peptide and protein binding. Biochemistry, 37(9):3187.

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