Probing the interaction of lysozyme with ciprofloxacin in the presence of different-sized Ag nano-particles by multispectroscopic techniques and isothermal titration calorimetry

Abstract

The binding of ciprofloxacin to lysozyme in the presence of three Ag nano-particles of varying sizes was for the first time investigated by multispectroscopic and isothermal titration calorimetry techniques at pH 7.4. The results indicated that ciprofloxacin quenched the fluorescence intensity of lysozyme through a static mechanism but in the presence of size-II Ag nano-particles, there were two kinds of interaction behaviors. The interaction between ciprofloxacin and lysozyme occurred via a second type of binding site, whereas in the presence of the Ag nano-particles, some changes occurred. The secondary structure of lysozyme–ciprofloxacin in the presence of Ag nano-particles was determined by circular dichroism. The thermodynamic parameters of the interaction between ciprofloxacin and lysozyme in the presence of Ag nano-particles were measured according to the van’t Hoff equation. The enthalpy (ΔH^○) and entropy (ΔS^○) changes were calculated to be −49.7 (kJ mol⁻¹) and −20.1 (J mol⁻¹ K⁻¹), respectively, which indicated that the interaction of ciprofloxacin with lysozyme was driven mainly by van der Waals forces and hydrogen bonding. In the presence of the three different-sized Ag nano-particles, the enthalpic and the entropic changes were both negative which indicated that hydrogen bonding with van der Waals forces played major roles in the binding between ciprofloxacin and lysozyme. Recent developments in nano-materials offer new pathways for controlling the protein behavior through surface interactions. These data indicate that the recent research on nano-particle/protein interactions will emphasize the importance of such interactions in biological systems with applications including the diagnosis and treatment of human diseases.

Keywords:

• lysozyme
• ciprofloxacin
• Ag nano-particles
• fluorescence spectroscopy
• circular dichroism
• isothermal titration calorimetry

Acknowledgments

The Research Council of the Mashhad Brunch, Islamic Azad University, Mashhad, Iran is gratefully acknowledged for financial support. The authors thank Dr Ljungberg for the English editing.