Study of characterization and application on the binding between 5-iodouridine with HSA by spectroscopic and modeling

• Published in: Carbohydrate polymers Vol. 73; no. 3; pp. 464 - 472
• Main Authors: Cui, Fengling, Zhang, Qiangzhai, Yan, Yinghua, Yao, Xiaojun, Qu, Guirong, Lu, Yan
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.08.2008; Elsevier Science
• Subjects: 5-Iodouridine; Applied sciences; Biological and medical sciences; Determination; Exact sciences and technology; Fluorescence quenching; Fundamental and applied biological sciences. Psychology; Human serum albumin (HSA); In solution. Condensed state. Thin layers; Modeling; Molecular biophysics; Natural polymers; Physico-chemical properties of biomolecules; Physicochemistry of polymers; Proteins; Synchronous fluorescence; 5-Iodouridine; Determination; Synchronous fluorescence; Human serum albumin (HSA); Modeling; Fluorescence quenching; Serum albumin; Experimental study; Iodine Organic compounds; Protein; Intermolecular interaction; Biological fixation; Salt effect; Molecular model; Binding mode; Nucleoside; Aqueous solution
• ISSN: 0144-8617; 1879-1344
• DOI: 10.1016/j.carbpol.2007.12.032

The binding of 5-iodouridine with human serum albumin was investigated under the simulative physiological conditions. The fluorescence spectra in combination with UV absorption and modeling method were used in the present work. A strong fluorescence quenching reaction of 5-iodouridine to HSA was observed and the quenching mechanism was suggested as static quenching procedure. The binding constants ( K) at different temperatures as well as thermodynamic parameters, enthalpy change (Δ H) and entropy change (Δ S), were calculated. It showed that the hydrophobic interaction was a predominant intermolecular force in order to stabilize the complex, which was in agreement with the result of modeling study. The binding distance between 5-iodouridine and HSA was calculated on the basis of the theory of Föster energy transfer. The effects of other ions on the binding constants were also discussed. Synchronous fluorescence spectroscopy (SFS) technique were successfully applied to determine protein in the biological samples.