Binding Characterization Study of the Interaction of an Anticancer Drug Ifosfamide with Bovine Serum Albumin

Authors

  • T.S. Rajendra Kumar Department of Chemistry, Rayalseema University, Kurnool, AP, India
  • M. Uma Mahesh Department of Chemistry, Rajeev Gandhi Memorial College of Engineering and Technology, Nandyal, India

Keywords:

Ifosfamide, BSA, UV-visible, Fluorescence, viscometry

Abstract

The interaction between Ifosfamide (IFO) and bovine serum albumin (BSA) has been studied. The studies were carried out in a buffer of medium at pH 7.4 using fluorescence spectroscopy, UV-vis spectroscopy, and Viscometric methods. The results of fluorescence quenching and UV-vis absorption spectra experiments indicated the formation of the complex of BSA-IFO. Binding parameters were determined using the Stern-Volmer equation. From fluorescence and UV-vis spectroscopic data, the binding constant between IFO and BSA was calculated to be 4.275 x 103 L mol-1 and 8.173 x 103 L mol-1 respectively. The results of thermodynamic parameters ∆G˚, ∆H˚ and ∆S˚ at different temperature indicate that the electrostatic interactions and also hydrogen bonds play a major role for IFO-BSA association.

 

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Published

2015-04-30

How to Cite

Kumar, T. R., & Mahesh, M. U. (2015). Binding Characterization Study of the Interaction of an Anticancer Drug Ifosfamide with Bovine Serum Albumin. International Journal of Scientific Research in Chemical Sciences, 5(1), 1–6. Retrieved from https://ijsrcs.isroset.org/index.php/j/article/view/33

Issue

Vol. 5 No. 1 (2018): April

Section

Research Article

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