Spectroscopic and molecular modeling studies of the interaction between cytidine and human serum albumin and its analytical application

✍ Scribed by Fengling Cui; Junli Wang; Xiaojun Yao; Li Wang; Qiangzhai Zhang; Guirong Qu

• Publisher: Wiley (John Wiley & Sons)
• Year: 2007
• Tongue: English
• Weight: 750 KB
• Volume: 87
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20815

✦ Synopsis

Abstract

In this study, the interaction between cytidine and human serum albumin (HSA) was investigated for the first time by fluorescence spectroscopy in combination with UV absorption spectrum and molecular modeling under simulative physiological conditions. Experimental results indicated that cytidine had a strong ability to quench the intrinsic fluorescence of human serum albumin. The binding constants (K) at different temperatures, thermodynamic parameter enthalpy changes (Δ__H__) and entropy changes (Δ__S__) of HSA‐cytidine had been calculated according to the relevant fluorescence data, which indicated that the hydrophobic and electrostatic interactions played a major role, which was in agreement with the results of molecular modeling study. In addition, the effects of other ions on the binding constants were also studied. Furthermore, synchronous fluorescence technology was successfully applied to the determination of human serum albumin added into the cytidine solution. © 2007 Wiley Periodicals, Inc. Biopolymers 87: 174–182, 2007.

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