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1 2009

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Binding of Cytidine-5'-monophosphate with Human Serum Albumin: Spectroscopic and Molecular Modeling Studies

Cui F. L., Yan Y. H., Zhang Q. Z., Du J., Yao X. J., Qu G. R., Lu Y.

Polish Journal of Chemistry

2009

Vol. 83, nr 10

1783-1795

The binding of cytidine-5’-monophosphate (CMP) to human serum albumin (HSA) was investigated by fluorescence spectroscopy in combination with molecular modeling under simulation of physiological conditions. The quenching mechanism was suggested to be static according to the fluorescence measurement. The thermodynamic parameters: enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be –5.09 kJ/mol and 73.00 J mol–1 K–1 according to the Vant’Hoff equation. These data suggest that hydrophobic inter actions are the predominant intermolecular forces stabilizing the complex. Experimental results are in agreement with the results obtained by molecular modeling study. In addition, the effects of commonions on the binding constants were also studied at room temperature.