Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 39, Issue 3, Pages 1004-1016Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2020.1733091
Keywords
Beta-lactoglobulin; astaxanthin; 5-fluorouracil; competitive binding; natural antioxidant
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Funding
- Hamadan University of Medical Sciences [9704122086]
- Kharazmi University
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In this study, the simultaneous carrier ability of β-LG for ATX and 5-FU was investigated using various spectroscopic techniques and molecular docking. The findings showed independent binding sites for ATX and 5-FU on the protein, with simultaneous binding enhancing protein stability to some extent.
In the present study, the simultaneous carrier ability of natural antioxidant of astaxanthin (ATX) and chemotherapeutic drug of 5-fluorouracil (5-FU) by whey protein of beta-lactoglobulin (beta-LG) using various spectroscopic techniques (UV-visible, fluorescence, circular dichroism (CD) and dynamic light scattering) in combination with molecular docking were investigated (at room and physiological temperatures). According to the fluorescence quenching tests, the binding parameters between drug and ATX with protein showed that the number of their binding sites was the same in the single and competitive states. Molecular docking results have showed completely consistent with the fluorescence data that presented the independent binding sites for 5-FU and ATX on beta-LG. Also, analysis of Far-UV-CD showed that the simultaneous binding of the drugs to the protein partially enhances its stability, which is associated with the decreasing in beta-sheet structure and increasing in alpha-helix. According to the Zeta potential measurements in the presence of different concentrations of the drugs, they have stronger binding to the protein at lower concentrations. Therefore, given the remarkable features of beta-LG, including the ability to interact simultaneously with the natural compound of ATX and the antitumor drug of 5-FU, this study could provide useful information for the development and improvement of new protein carrier systems with synergism potency. Communicated by Ramaswamy H. Sarma
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