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

被引:29
作者
Fan J.C. [1 ]
Chen X. [1 ]
Wang Y. [1 ]
Fan C.P. [1 ]
Shang Z.C. [1 ]
机构
[1] Department of Chemistry, Zhejiang University, Hangzhou
基金
中国国家自然科学基金;
关键词
Pefloxacin mesylate (PFLX); Bovine lactoferrin (BLf); Human serum albumin (HSA); Fluorescence spectra; Energy-transfer efficiency; O657.3;
D O I
10.1631/jzus.2006.B0452
中图分类号
学科分类号
摘要
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.
引用
收藏
页码:452 / 458
页数:6
相关论文
共 55 条
[1]  
Aguila A.(2001)Lactoferrin: antimicrobial and diagnostic properties Biotechnology Apply 18 76-83
[2]  
Brock J.H.(1998)Three-dimensional structure of lactoferrin—Implications for function, including comparisons with transferring Advances in Experimental Medicine and Biology 443 1-14
[3]  
Baker E.N.(1998)Effect of BSA binding on photophysical and photochemical properties of triarylmethane dyes Journal of Physical Chemistry B 102 4678-40
[4]  
Anderson B.F.(1999)Expanded activity and utility of the new fluoroquinolones: a review Clinical Therapeutics 21 3-1279
[5]  
Baker H.M.(1993)The binding interaction of Coomassie Blue with proteins Analytical Biochemistry 213 407-undefined
[6]  
MacGillivray R.T.A.(1970)Analysis of macromolecule-ligand binding by determination of stepwise equilibrium constants Biochemistry 9 4580-undefined
[7]  
Moore S.A.(1981)Lanthanide ion luminescence probes. Measurement of distance between intrinsic protein fluorophores and bound metal ions: quantiation of energy transfer between tryptophan and terbium (III) or europium (III) in the calcium-binding protein parvalbumin J. Am. Chem. Soc. 103 2856-undefined
[8]  
Peterson N.A.(2002)Study of the interaction between terazosin and serum albumin: synchronous fluorescence determination of terazosin Analytica Chimica Acta 452 185-undefined
[9]  
Shewry S.C.(1971)Properties of graphical representations of multiple classes of binding sites Biochemistry 10 3065-undefined
[10]  
Tweedie J.W.(1990)Interaction of bovine lactoferrin with other proteins of milk whey International Journal of Biological Macromolecules 12 2-undefined