메뉴 건너뛰기




Volumn 39, Issue 5, 2010, Pages 709-717

Investigation of the interaction between ofloxacin and bovine serum albumin: Spectroscopic approach

Author keywords

Binding distance; Bovine serum albumin; Fluorescence quenching; Ofloxacin; Thermodynamic parameters

Indexed keywords


EID: 77954877963     PISSN: 00959782     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10953-010-9527-8     Document Type: Article
Times cited : (27)

References (28)
  • 1
    • 37349019737 scopus 로고    scopus 로고
    • Ofloxacin induces apoptosis in mi-croencapsulated juvenile rabbit chondrocytes by caspase-8-dependent mitochondrial pathway
    • Sheng, Z., Cao, X., Peng, S., Wang, C., Li, Q., Wang, Y., Liu, M.: Ofloxacin induces apoptosis in mi-croencapsulated juvenile rabbit chondrocytes by caspase-8-dependent mitochondrial pathway. Toxicol. Appl. Pharmacol. 226, 119-127 (2008)
    • (2008) Toxicol. Appl. Pharmacol. , vol.226 , pp. 119-127
    • Sheng, Z.1    Cao, X.2    Peng, S.3    Wang, C.4    Li, Q.5    Wang, Y.6    Liu, M.7
  • 2
    • 11144341431 scopus 로고    scopus 로고
    • Determination of fluoroquinolone antibiotics in waste-water effluents by liquid chromatography-mass spectrometry and fluorescence detection
    • Nakata, H., Kannan, K., Jones, P. D., Giesy, J. P.: Determination of fluoroquinolone antibiotics in waste-water effluents by liquid chromatography-mass spectrometry and fluorescence detection. Chemosphere 58, 759-766 (2005)
    • (2005) Chemosphere , vol.58 , pp. 759-766
    • Nakata, H.1    Kannan, K.2    Jones, P.D.3    Giesy, J.P.4
  • 3
    • 0036592241 scopus 로고    scopus 로고
    • Physicochemical properties of quinolone antibiotics in various environments
    • Park, H. R., Kim, T. H., Bark, K. M.: Physicochemical properties of quinolone antibiotics in various environments. Eur. J. Med. Chem. 37, 443-460 (2002)
    • (2002) Eur. J. Med. Chem. , vol.37 , pp. 443-460
    • Park, H.R.1    Kim, T.H.2    Bark, K.M.3
  • 4
    • 0035871938 scopus 로고    scopus 로고
    • Stereoselective determination of ofloxacin and its metabolites in human urine by capillary electrophoresis using laser-induced fluorescence detection
    • DOI 10.1016/S0378-4347(00)00595-8, PII S0378434700005958
    • Horstkötter, C., Blaschke, G.: Stereoselective determination of ofloxacin and its metabolites in human urine by capillary electrophoresis using laser-induced fluorescence detection. J. Chromatogr. B 754, 169-178 (2001) (Pubitemid 32241082)
    • (2001) Journal of Chromatography B: Biomedical Sciences and Applications , vol.754 , Issue.1 , pp. 169-178
    • Horstkotter, C.1    Blaschke, G.2
  • 5
    • 69649084169 scopus 로고    scopus 로고
    • Ofloxacin targeting to lungs by way of microspheres
    • Sree, H., Chandramouli, R., Shobha, R.: Ofloxacin targeting to lungs by way of microspheres. Int. J. Pharm. 380, 127-132 (2009)
    • (2009) Int. J. Pharm. , vol.380 , pp. 127-132
    • Sree, H.1    Chandramouli, R.2    Shobha, R.3
  • 6
    • 62249093042 scopus 로고    scopus 로고
    • Phar-macokinetics of fluoroquinolones in critical care patients: A bio-analytical HPLC method for the simultaneous quantification of ofloxacin, ciprofloxacin and moxifloxacin in human plasma
    • Smet, J. D., Boussery, K., Colpaert, K., Sutter, P. D., Paepe, P. D., Decruyenaere, J., Bocxlaer, J. V.: Phar-macokinetics of fluoroquinolones in critical care patients: A bio-analytical HPLC method for the simultaneous quantification of ofloxacin, ciprofloxacin and moxifloxacin in human plasma. J. Chromatogr. B 877, 961-967 (2009)
    • (2009) J. Chromatogr. B. , vol.877 , pp. 961-967
    • Smet, J.D.1    Boussery, K.2    Colpaert, K.3    Sutter, P.D.4    Paepe, P.D.5    Decruyenaere, J.6    Bocxlaer, J.V.7
  • 7
    • 47049128634 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of ofloxacin sustained release pellets
    • Cui, Y., Zhang, Y., Tang, X.: In vitro and in vivo evaluation of ofloxacin sustained release pellets. Int. J. Pharm. 360, 47-52 (2008)
    • (2008) Int. J. Pharm. , vol.360 , pp. 47-52
    • Cui, Y.1    Zhang, Y.2    Tang, X.3
  • 8
    • 27744534569 scopus 로고    scopus 로고
    • Effects of hepatic fibrosis on ofloxacin pharmacokinetics in rats
    • DOI 10.1016/j.phrs.2005.08.005, PII S1043661805001556
    • Wang, H., Liao, Z. X., Chen, M., Hu, X. L.: Effects of hepatic fibrosis on ofloxacin pharmacokinetics in rats. Pharm. Res. 53, 28-34 (2006) (Pubitemid 41619376)
    • (2006) Pharmacological Research , vol.53 , Issue.1 , pp. 28-34
    • Wang, H.1    Liao, Z.-X.2    Chen, M.3    Hu, X.-L.4
  • 9
    • 2442573792 scopus 로고    scopus 로고
    • Supercritical fluid extraction of the fluoroquinolones norfloxacin and ofloxacin from orally treated-chicken breast muscles
    • Shen, J. Y., Kim, M. R., Lee, C. J., Kim, I. S., Lee, K. B., Shim, J. H.: Supercritical fluid extraction of the fluoroquinolones norfloxacin and ofloxacin from orally treated-chicken breast muscles. Anal. Chim. Acta 513, 451-455 (2004)
    • (2004) Anal. Chim. Acta , vol.513 , pp. 451-455
    • Shen, J.Y.1    Kim, M.R.2    Lee, C.J.3    Kim, I.S.4    Lee, K.B.5    Shim, J.H.6
  • 11
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M., Carter, D. C.: Atomic structure and chemistry of human serum albumin. Nature 358, 209-215 (1992)
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 12
    • 77956725742 scopus 로고    scopus 로고
    • Plasma protein binding of drugs
    • Olson, R. E., Christ, D. D.: Plasma protein binding of drugs. Ann. Rep. Med. Chem. 31, 327-336 (1996)
    • (1996) Ann. Rep. Med. Chem. , vol.31 , pp. 327-336
    • Olson, R.E.1    Christ, D.D.2
  • 13
    • 0028558671 scopus 로고
    • Preliminary crystallographic studies of four crystal forms of serum albumin
    • Carter, D. C., Chang, B., Ho, J. X., Keeling, K., Krishnasami, Z.: Preliminary crystallographic studies of four crystal forms of serum albumin. Eur. J. Biochem. 226, 1049-1052 (1994)
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1049-1052
    • Carter, D.C.1    Chang, B.2    Ho, J.X.3    Keeling, K.4    Krishnasami, Z.5
  • 14
    • 0034602966 scopus 로고    scopus 로고
    • Conformational transitions of the three recombinant domains of human serum albumin depending on pH
    • Dockal, M., Carter, D. C., Rüker, F.: Conformational transitions of the three recombinant domains of human serum albumin depending on pH. J. Biol. Chem. 275, 3042-3050 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 3042-3050
    • Dockal, M.1    Carter, D.C.2    Rüker, F.3
  • 15
    • 68749119350 scopus 로고    scopus 로고
    • Interaction between levamisole hydrochloride and bovine serum albumin and the influence of alcohol: Spectra
    • Yan, H., Zhao, S., Yang, J., Zhu, X., Dai, G., Liang, H., Pan, F., Weng, L.: Interaction between levamisole hydrochloride and bovine serum albumin and the influence of alcohol: Spectra. J. Solution Chem. 38, 1183-1192 (2009)
    • (2009) J. Solution Chem. , vol.38 , pp. 1183-1192
    • Yan, H.1    Zhao, S.2    Yang, J.3    Zhu, X.4    Dai, G.5    Liang, H.6    Pan, F.7    Weng, L.8
  • 17
    • 65249134878 scopus 로고    scopus 로고
    • Investigation of the interaction between berberine and human serum albumin
    • Hu, Y. J., Liu, Y., Xiao, X. H.: Investigation of the interaction between berberine and human serum albumin. Biomacromolecules 10, 517-521 (2009)
    • (2009) Biomacromolecules , vol.10 , pp. 517-521
    • Hu, Y.J.1    Liu, Y.2    Xiao, X.H.3
  • 18
    • 41949108321 scopus 로고    scopus 로고
    • Molecular interactions between Wells-Dawson type polyoxometalates and human serum albumin
    • DOI 10.1021/bm701120j
    • Zhang, G., Keita, B., Craescu, C. T., Miron, S., Oliveira, P., Nadjo, L.: Molecular interactions between Wells-Dawson type polyoxometalates and human serum albumin. Biomacromolecules 9, 812-817 (2008) (Pubitemid 351560470)
    • (2008) Biomacromolecules , vol.9 , Issue.3 , pp. 812-817
    • Zhang, G.1    Keita, B.2    Craescu, C.T.3    Miron, S.4    De Oliveira, P.5    Nadjo, L.6
  • 20
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S. S.: Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10, 3254-3263 (1971)
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 21
    • 60549105999 scopus 로고    scopus 로고
    • In vitro study on the interaction between thiophanate methyl and human serum albumin
    • Li, J., Liu, X., Ren, C., Li, J., Sheng, F., Hu, Z.: In vitro study on the interaction between thiophanate methyl and human serum albumin. J. Photochem. Photobiol., B Biol. 94, 158-163 (2009)
    • (2009) J. Photochem. Photobiol., B. Biol. , vol.94 , pp. 158-163
    • Li, J.1    Liu, X.2    Ren, C.3    Li, J.4    Sheng, F.5    Hu, Z.6
  • 22
    • 0035818919 scopus 로고    scopus 로고
    • Cheminformatic models to predict binding affinities to human serum albumin
    • Colmenarejo, G., Alvarez-Pedraglio, A., Lavandera, J. L.: Cheminformatic models to predict binding affinities to human serum albumin. J. Med. Chem. 44, 4370-4378 (2001)
    • (2001) J. Med. Chem. , vol.44 , pp. 4370-4378
    • Colmenarejo, G.1    Alvarez-Pedraglio, A.2    Lavandera, J.L.3
  • 23
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P. D., Subramanian, S.: Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry 20, 3096-3102 (1981)
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 24
    • 0010714008 scopus 로고
    • Thermodynamics of protein interactions
    • H. Peeters ed., Pergamon, Oxford
    • Timaseff, S. N.: Thermodynamics of protein interactions. In: H. Peeters (ed.), Proteins of Biological Fluids. Pergamon, Oxford (1972)
    • (1972) Proteins of Biological Fluids
    • Timaseff, S.N.1
  • 25
    • 69049115141 scopus 로고    scopus 로고
    • Site-specific two-color protein labeling for FRET studies using split inteins
    • Yang, J. Y., Yang, W. Y.: Site-specific two-color protein labeling for FRET studies using split inteins. J. Am. Chem. Soc. 131, 11644-11645 (2009)
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 11644-11645
    • Yang, J.Y.1    Yang, W.Y.2
  • 27
    • 43949133853 scopus 로고    scopus 로고
    • Gaining an insight into the photore-activity of a drug in a protein environment: A case study on nalidixic acid and serum albumin
    • Monti, S., Manet, I., Manoli, F., Capobianco, M. L., Marconi, G.: Gaining an insight into the photore-activity of a drug in a protein environment: A case study on nalidixic acid and serum albumin. J. Phys. Chem. B 112, 5742-5754 (2008)
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 5742-5754
    • Monti, S.1    Manet, I.2    Manoli, F.3    Capobianco, M.L.4    Marconi, G.5
  • 28
    • 0005885530 scopus 로고
    • Recent advances in molecular luminescence analysis
    • Miller, J. N.: Recent advances in molecular luminescence analysis. Proc. Anal. Div. Chem. Soc. 16, 203-208 (1979)
    • (1979) Proc. Anal. Div. Chem. Soc. , vol.16 , pp. 203-208
    • Miller, J.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.