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

T.S. Rajendra Kumar¹ , M. Uma Mahesh²

1. Department of Chemistry, Rayalseema University, Kurnool, AP, India.
2. Department of Chemistry, Rajeev Gandhi Memorial College of Engineering and Technology, Nandyal, India.

Correspondence should be addressed to: tsrajendrakumar2017@gmail.com.

Section:Research Paper, Product Type: Isroset-Journal
Vol.5 , Issue.1 , pp.1-6, Apr-2018

CrossRef-DOI:   https://doi.org/10.26438/ijsrcs/v5i1.16

Online published on May 30, 2018

Copyright © T.S. Rajendra Kumar, M. Uma Mahesh . This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
 

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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.

Key-Words / Index Term :
Ifosfamide, BSA, UV-visible, Fluorescence, viscometry

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