Effect of Temperature and Additives on the Interaction of Ciprofloxacin Hydrochloride Drug with Polyvinylpyrrolidone and Bovine Serum Albumin: Spectroscopic and Molecular Docking Study

• Published in: Journal of Oleo Science 2021, Vol.70(3), pp.397-407
• Main Authors: Mukta, Nusrat Jahan, Mahbub, Shamim, Abedin, Md. Joynal, Hossain, Md. Emdad, Kumar, Dileep, Hoque, Md. Anamul, Khan, Mohammed Abdullah, Rehman, Md. Tabish, Azum, Naved, Akram, Mohd, Marwani, H.M.
• Format: Article
• Language: English
• Subjects: Acetic acid; Additives; antibiotic drug; Antibiotics; Aqueous solutions; Bacterial diseases; binding constant; Binding sites; Biopolymers; bovine serum albumin; Complex formation; Complexation; Enthalpy; Entropy; Fluorescence; Gibbs free energy; Mathematical analysis; Molecular docking; polymer; Polyvinylpyrrolidone; Quenching; Serum albumin; Spectroscopic analysis; Temperature effects; thermodynamics
• ISSN: 1345-8957; 1347-3352
• DOI: 10.5650/jos.ess20306

The fluoroquinolone antibiotic drug namely ciprofloxacin hydrochloride (CFH) is widely prescribed for the treatment of different bacterial infections. The interaction of CFH with a synthetic polymer, polyvinyl pyrrolidone (PVP), and biopolymer, bovine serum albumin (BSA) was studied by UVvisible and fluorescence spectroscopic methods at different temperatures. The binding constant (K b ) for the CFH-PVP complex was determined from the Benesi-Hildebrand plot. PVP of different molecular weights (MW) (such as 24,000, 40,000, 360,000, and 700,000 g. mole-1) were used for the interaction between CFH and PVP. The gradual increase in K b value and the complexation reaction was found to be much enhanced with the augmentation of the MW of PVP. The values of K b were also found to be increased with increasing temperatures as well as with the increase of electrolyte/acetic acid concentration. The Gibbs free energy of binding (∆G 0) values of the interaction process was negative which indicates the complex formation is thermodynamically spontaneous. The positive values of enthalpy (∆H 0) and entropy (∆S 0) of binding connote that the binding force for CFH-PVP complexation is hydrophobic in nature and the complexation is entropy controlled. The negative intrinsic enthalpy (∆H *,0) values indicate the high stability of CFH-PVP complexes. Molecular docking calculation discloses the existence of similar binding forces between CFH and PVP obtained by the analysis of experimental data from UV-visible spectroscopic method. The binding constant between CFH and BSA (K b ), quenching constant (K sv ), the number of binding sites (n), and the quenching rate constant (K q ) for the CFH-BSA system were also calculated. The values of K sv , K q , and n for the CFH-BSA system are lower in 0.05 mol L-1 urea solution and higher in PVP solutions compared to those of aqueous medium.