A study on the interaction of two chemotherapeutic drugs of Oxali-Palladium and 5- Fluorouracil simultaneously with milk carrier protein of β-lactoglobulin

βLG is a basic element of globular protein carrier, which is the major protein in the whey of ruminantmilk and is of main interest in the dairy industry. In the present study, the effects of 5-fluorouracil andoxali-palladium, as anticancer drugs, on the structure and function of βLG were investigated usingdifferent spectroscopic methods of fluorescence and circular dichroism (CD) at two temperatures of 25and 37 °C. The resulted data from intrinsic fluorescence spectra of protein indicated that 5-Fluorouraciland oxalli-Palladium can quench the fluorescence intensity of βLG in dose-dependent manner via staticmechanism of fluorescence quenching. Analysis of quenching data have represented that there are 2 and 1binding sites on βLG for binding of oxali-palladium and 5-Fluorouracil, respectively at two temperaturesof 25 and 37 °C. The analysis of circular dichroic spectra indicated reduction in stability of protein andchanged the secondary structure of protein with reduction of α helical structure and increasing of β sheetstructure. As a result, it can be concluded that both of the chemotherapeutic drugsof oxali-Palladium and5-fluorouracil can bind to carrier protein of βLG and changed the secondary and tertiary structures ofprotein which can be considered as side effects of them.

کلیدواژه ها:

5-fluorouracil ، Oxali-palladium ، β-lactoglobulin ، fluorescence ، circular dichroism