Spectroscopic and molecular modeling studies of the interaction between cytidine and human serum albumin and its analytical application.
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 (DeltaH) and entropy changes (DeltaS) 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.
Cui
Fengling
F
Key Laboratory for Environmental Pollution Control Technology of Henan Province, School of Chemistry and Environmental Science, Henan Normal University, Xinxiang, China. fenglingcui@hotmail.com
Wang
Junli
J
Yao
Xiaojun
X
Wang
Li
L
Zhang
Qiangzhai
Q
Qu
Guirong
G
D003562:Cytidine / Q000737:chemistry*; D019277:Entropy; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D012709:Serum Albumin; D003562:Cytidine