Abstract

The interaction between bovine serum albumin (BSA) and prulifloxacin was investigated by ultraviolet spectrophotometer (UV) and fluorescence spectroscopy in this paper. Two-dimensional (2D) correlation spectroscopy was applied to the analysis of fluorescence spectra. The results of spectroscopic measurements suggested that prulifloxacin (PL) have a strong ability to quench the intrinsic fluorescence of bovine serum albumin through static quenching procedure. Thermodynamic parameter enthalpy changes (ΔH) and entropy changes (ΔS) were calculated. Owing to the spectral resolution enhancement in 2D correlation spectroscopy, the structure change of prulifloxacin can be observed.

Highlights

  • IntroductionPrulifloxacin (Fig. 1), the prodrug of ulifloxacin (AF3013, NM394), is a broad-spectrum oral fluoroquinolone antibacterial agent [11]

  • Prulifloxacin (Fig. 1), the prodrug of ulifloxacin (AF3013, NM394), is a broad-spectrum oral fluoroquinolone antibacterial agent [11].Serum albumins are one of the most abundant proteins in blood plasma

  • We investigated the interaction between prulifloxacin and bovine serum albumin by fluorescence spectroscopy, and revealed that hydrophobic interaction plays an important role in the binding between prulifloxacin and BSA

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Summary

Introduction

Prulifloxacin (Fig. 1), the prodrug of ulifloxacin (AF3013, NM394), is a broad-spectrum oral fluoroquinolone antibacterial agent [11]. Spectroscopic method has been widely applied in investigating drug binding with albumin under physiological conditions because of its accuracy, sensitivity, rapidity and convenience of usage [10,19]. We investigated the interaction between prulifloxacin and bovine serum albumin by fluorescence spectroscopy, and revealed that hydrophobic interaction plays an important role in the binding between prulifloxacin and BSA. We analyzed fluorescence spectra by 2D [4,6,13,14,15,16,17] correlation fluorescence spectroscopy to reveal the details of binding interaction between prulifloxacin and BSA. Using the 2D spectroscopy, it is possible to probe the specific order of chemical functional changes upon perturbation, perform detailed dynamics study of molecule vibration

Materials
Equipments and spectral measurements
Principles of fluorescence quenching
Fluorescence quenching
Binding site and binding constant
Thermodynamic parameters and nature of the binding forces
Conclusion
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