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.
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The application of fluorescence spectroscopy methods to determining the properties of camptothecins promising anticancer agents are described in this paper. The fluorescence anisotropy measurements provide useful information about the binding of camptothecin and its analogues to cell membranes and human serum albumin (HSA) that is important for potential clinical applications of these agents, and permits the selection from many camptothecin analogues those ones exhibiting desirable biomedical properties. Binding properties of 7-trimethylsilyl-ethyl-10 hydroxy-camptothecin are the subject of this paper.
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