ABSTRACT
The binding of anticancer drugs (i) Uracil (U), (ii) 5-Fluorouracil (5FU) and (iii) 5-Chlorouracil (5ClU), to bovine serum albumin (BSA) at two levels of temperature was studied by the fluorescence of quenching method. UV/Vis, time-resolved fluorescence, Fourier transform infrared spectroscopy (FTIR), proton nuclear magnetic resonance ((1)H NMR) and scanning electron microscope (SEM) analyses were also made. Binding constants (K(a)) and binding sites (n) at various levels of temperature were calculated. The obtained binding sites were found to be equal to one for all the three quenchers (U, 5FU and 5ClU) at two different temperature levels. Thermodynamic parameters ΔH, ΔG and ΔS have been calculated and were presented in tables. Change in FTIR absorption intensity shows strong binding of anticancer drugs to BSA. Changes in chemical shifts of NMR and fluorescence lifetimes of the drugs indicate the presence of interaction and binding of BSA to anticancer drugs. (1)H NMR spectra and SEM photographs also conform this binding.
Subject(s)
Antineoplastic Agents/metabolism , Serum Albumin, Bovine/metabolism , Animals , Antineoplastic Agents/analysis , Antineoplastic Agents/chemistry , Binding Sites , Cattle , Fluorouracil/chemistry , Fluorouracil/metabolism , Kinetics , Magnetic Resonance Spectroscopy , Protein Binding , Serum Albumin, Bovine/analysis , Serum Albumin, Bovine/chemistry , Serum Albumin, Bovine/ultrastructure , Spectrophotometry, Ultraviolet , Spectroscopy, Fourier Transform Infrared , Temperature , Time Factors , Uracil/analogs & derivatives , Uracil/chemistry , Uracil/metabolismABSTRACT
The interactions between potassium mono and di phosphates and bovine serum albumin (BSA) were studied using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The experimental results showed that the potassium mono and di phosphates could insert into the BSA and quench the inner fluorescence of BSA by forming the potassium mono phosphate-BSA and pottassium di phosphate-BSA complexes. It was found that the static quenching was the main reason leading to the fluorescence quenching. It was conformed by XRD and SEM techniques.
