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[Interaction between protein and ciprofloxacin].

H He1, J S Yu, S P Xu

  • 1Deparment of Analytical Chemistry, China Pharmaceutical University, Nanjing 210009, China.

Yao Xue Xue Bao = Acta Pharmaceutica Sinica
|February 15, 2003
PubMed
Summary
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Fluorescence spectroscopy reveals that ciprofloxacin binds to bovine serum albumin (BSA) via Van der Waals forces, indicating BSA can transport the drug in vivo and altering protein structure.

Area of Science:

  • Biochemistry
  • Pharmacology

Background:

  • Bovine serum albumin (BSA) is a primary carrier protein in blood plasma.
  • Understanding drug-protein interactions is crucial for pharmacokinetics and drug efficacy.

Purpose of the Study:

  • To investigate the binding interaction between ciprofloxacin and BSA using fluorescence spectroscopy.
  • To determine the binding constants and thermodynamic parameters of the ciprofloxacin-BSA complex.

Main Methods:

  • Fluorescence spectroscopy was employed to monitor the interaction.
  • Binding constants were calculated using a Lineweaver-Burk plot.
  • Thermodynamic parameters were analyzed to identify binding forces.

Main Results:

  • A binding constant of approximately 10(4) was observed at 26°C and 45°C.

Related Experiment Videos

  • Thermodynamic parameters (ΔH = -49.13 kJ/mol, ΔG = -26.45 kJ/mol, ΔS = -75 J/mol) indicate spontaneous binding.
  • A shift in BSA's synchronous fluorescence spectra suggests ciprofloxacin alters protein conformation.

    • Conclusions:

    • Fluorescence energy transfer occurs between ciprofloxacin and BSA.
    • Van der Waals interactions are the primary binding force.
    • BSA facilitates in vivo transport and is conformationally affected by ciprofloxacin.