Thermochemistry Study on Interaction Between Anti-tumor Drug Tegafur and Bovine Serum Albumin

Abstract

Abstract: From the assumptions of this binding system and the Langmuir's binding theory, the interaction between tegafur and bovine serum albumin(BSA) was investigated by the nano-watt-scale isothermal titration calorimetry and the circular dichroism(CD) spectrometry at 298.15 K. The results show that there are two classes of binding sites on the protein BSA for tegafur. For the first class of binding, the binding site number is N=52.00±0.12, the binding constant is K=(9.83±0.13)×10⁴ L/mol, the binding enthalpy is ΔH=(30.10±0.17) kJ/mol, the binding entropy is ΔS=(196.00±0.65) J/(mol·K), and the binding Gibbs free energy is ΔG=(-28.50±0.66) kJ/mol. This binding is an entropy driven process, and the hydrophobic interaction is the main motive-force for the process. For the second class of binding, the binding sites number is N=86.00±0.14, the binding constant is K=(9.35±0.13)×10⁴ L/mol, the binding enthalpy is ΔH=(-19.80±0.17) kJ/mol, the binding entropy is ΔS=(28.30±0.50) J/(mol·K), and the binding Gibbs free energy is ΔG=(-28.40±0.43) kJ/mol. This binding is an enthalpy-entropy synergically driven process, and the hydrogen bond and electrostatic interactions are the main motive-force for the process. The analytical results of circular dichroism(CD) spectra show that the interactions between tegafurl and BSA resulted in the change of the relative contents of secondary structure units of protein BSA in these two classes of the binding processes. The thermodynamic effects of the binding system are integrated results which come from different interactional effects in the binding process. The conformations of the protein BSA underwent changes induced by the anti-tumor drug tegafurl in the solution medium of this binding system.

Key words: Tegafur, Bovine serum albumin, Isothermal titration calorimetry, Circular dichroism spectrometry

CLC Number:

O642

TrendMD:

LI Lin-Wei*, WANG Dong-Dong, SUN De-Zhi, WEI Xin-Ting, LIU Min, ZHAO Qiang. Thermochemistry Study on Interaction Between Anti-tumor Drug Tegafur and Bovine Serum Albumin[J]. Chem. J. Chinese Universities, doi: .

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Thermochemistry Study on Interaction Between Anti-tumor Drug Tegafur and Bovine Serum Albumin

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