Full Text:   <2205>

CLC number: O657.3

On-line Access: 

Received: 2005-08-10

Revision Accepted: 2005-12-19

Crosschecked: 0000-00-00

Cited: 18

Clicked: 4951

Citations:  Bibtex RefMan EndNote GB/T7714

-   Go to

Article info.
1. Reference List
Open peer comments

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

http://doi.org/10.1631/jzus.2006.B0452


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.

@article{title="Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin",
author="FAN Ji-cai, CHEN Xiang, WANG Yun, FAN Cheng-ping, SHANG Zhi-cai",
journal="Journal of Zhejiang University Science B",
volume="7",
number="6",
pages="452-458",
year="2006",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2006.B0452"
}

%0 Journal Article
%T Binding interactions of pefloxacin mesylate with bovine lactoferrin and human serum albumin
%A FAN Ji-cai
%A CHEN Xiang
%A WANG Yun
%A FAN Cheng-ping
%A SHANG Zhi-cai
%J Journal of Zhejiang University SCIENCE B
%V 7
%N 6
%P 452-458
%@ 1673-1581
%D 2006
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2006.B0452

TY - JOUR
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
J0 - Journal of Zhejiang University Science B
VL - 7
IS - 6
SP - 452
EP - 458
%@ 1673-1581
Y1 - 2006
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2006.B0452


Abstract: 
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

Reference

[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.

Open peer comments: Debate/Discuss/Question/Opinion

<1>

Please provide your name, email address and a comment





Journal of Zhejiang University-SCIENCE, 38 Zheda Road, Hangzhou 310027, China
Tel: +86-571-87952783; E-mail: cjzhang@zju.edu.cn
Copyright © 2000 - 2022 Journal of Zhejiang University-SCIENCE