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

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 obs...

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Published inCarbohydrate 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
LanguageEnglish
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
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Abstract 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.
AbstractList 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.
Author Zhang, Qiangzhai
Cui, Fengling
Lu, Yan
Qu, Guirong
Yan, Yinghua
Yao, Xiaojun
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Issue 3
Keywords 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
Language English
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Elsevier Science
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Snippet The binding of 5-iodouridine with human serum albumin was investigated under the simulative physiological conditions. The fluorescence spectra in combination...
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StartPage 464
SubjectTerms 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
Title Study of characterization and application on the binding between 5-iodouridine with HSA by spectroscopic and modeling
URI https://dx.doi.org/10.1016/j.carbpol.2007.12.032
Volume 73
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