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Probing of the Interaction Between Β-Lactoglobulin and the Anticancer Drug Oxaliplatin Publisher Pubmed



Ghalandari B1 ; Divsalar A2 ; Eslamimoghadam M3 ; Saboury AA4, 5 ; Haertle T6 ; Amanlou M7 ; Parivar K1
Authors
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Authors Affiliations
  1. 1. Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
  2. 2. Department of Biological Sciences, Kharazmi University, Tehran, Iran
  3. 3. Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
  4. 4. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
  5. 5. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran
  6. 6. Fonctions et Interactions des Proteines, Biopolymeres, Interactions, Associations, Institut National de la Recherche Agronomique, Nantes, France
  7. 7. Department of Medicinal Chemistry and Drug Design and Development Research Center, Tehran University of Medical Sciences, Tehran, Iran

Source: Applied Biochemistry and Biotechnology Published:2015


Abstract

The potential carrier role of β-lactoglobulin (β-LG) and its interactions with oxaliplatin were studied using various spectroscopic techniques (fluorescence, UV–visible, and circular dichroism (CD)) in an aqueous medium at two temperatures of 25 and 37 °C in combination with a molecular docking study. Fluorescence measurements have shown that the observed quenching is a combination of static and dynamic quenching with a predominant contribution of static mode. The presence of a single binding site located in the internal cavity of the β-barrel of β-LG was confirmed by molecular docking calculations. Thermodynamic data as well as molecular docking indicated that the hydrophobic interactions dominate in the binding site. Results of fluorescence resonance energy transfer (FRET) measurements in combination with docking results imply that resonance energy transfer occurs between β-LG and its ligand oxaliplatin. Additionally, CD results revealed that oxaliplatin binding has no influence on the β-LG structure. The molecular docking results indicate that docking may be an appropriate method for the prediction and confirmation of experimental results. Complementary molecular docking results may be useful for the determination of the binding mechanism of proteins such as β-LG in pharmaceutical and biophysical studies providing new insight in the novel pharmacology and new solutions in the formulation of advanced oral drug delivery systems. © 2014, Springer Science+Business Media New York.