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

• Autorzy: Cui F. L. , Yan Y. H. , Zhang Q. Z. , Du J. , Yao X. J. , Qu G. R. , Lu Y.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

cytidine-5'-monophosphate (CMP),; human serum albumin (HSA); fluorescence spectroscopy; synchronous fluorescence spectrum; molecular modeling

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Polish Journal of Chemistry
• Rocznik: 2009
• Tom: Vol. 83, nr 10
• Strony: 1783--1795
• Opis fizyczny: Bibliogr. 34 poz., rys.

Twórcy

autor

Cui F. L.

autor

Yan Y. H.

autor

Zhang Q. Z.

autor

Du J.

autor

Yao X. J.

autor

Qu G. R.

autor

Lu Y.

• School of Chemistry and Environmental Science, Key Laboratory for Yellow River and Huai he River Water Environment and Pollution Control Ministry of Education, Henan Normal University, Xinxiang 453007, P.R. China,

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