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Comparing the Interactions and Structural Changes in Milk Carrier Protein of -Lactoglobulin upon Binding of 5-Fluorouracil and Oxali-palladium


 Start Page 28 | End Page 34


 β , lactoglobulin (β , LG) is the major protein in the whey of ruminant milk and it can be used as a carrier for anticancer drugs. In this study, the comparison interaction of two chemotherapeutic anti, cancer drugs of 5, Fluorouracil and oxali, palladium with milk carrier protein of β , LG was investigated using Fluorescence spectroscopy. The analysis of Fluorescence spectra showed that the addition of the 5, Fluorouracil and oxali, palladium to β , LG solution led to a significant reduction in the intrinsic Fluorescence spectra of protein and then quenched it. The binding sites and thermodynamic parameters of 5, Fluorouracil and oxali, palladium on the protein were calculated by analyzing of van’ t Hoff equation at different temperatures. Binding results have represented that there are 2 and 1binding sites on β , LG for binding of 5, Fluorouracil and oxali, palladium at physiological temperature, respectively. According to the results, van der Waals and hydrogen bonding have the main role of the interactions of β , LG with oxali, palladium, while electrostatic interactions have a major role in the interaction of β , LG with 5, Fluorouracil. Finally, regard to the above results, it can be concluded that the anticancer drugs of 5, Fluorouracil and oxali, palladium can bind to the carrier protein of β , LG and changed the structure of it differently.


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