Evaluation of binding and thermodynamic characteristics of interactions between a citrus flavonoid hesperitin with protein and effects of metal ions on binding

Ashwini H. Hegde, B. Sandhya, J. Seetharamappa

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The mechanism of interaction of a non-glycosidic citrus flavonoid, hesperitin (HES) with bovine serum albumin (BSA) was studied by UV-vis absorption, fluorescence, FT-IR, circular dichroism, fluorescence anisotropy and synchronous fluorescence spectroscopy in phosphate buffer of pH 7.4. Fluorescence data revealed that the fluorescence quenching of BSA by HES was the result of the formed complex of HES-BSA. The binding constants and thermodynamic parameters at four different temperatures, the location of binding, and the nature of binding force were determined. The hydrogen bonds interactions were found to be the predominant intermolecular forces to stabilize the complex. The conformation of BSA was discussed by synchronous fluorescence and CD methods. The alterations of protein secondary structure upon complexation with HES were evident from the gradual decrease in a-helicity. The distance between the donor (BSA) and acceptor (flavonoid) was calculated from the fluorescence resonance energy transfer and found to be 1.978 nm. Common ions viz., Zn 2+, K +, Cu 2+, Ni 2+, Mn 2+ and Co 2+ were found to influence the binding of flavonoid to protein.

Original languageEnglish
Pages (from-to)4921-4929
Number of pages9
JournalMolecular Biology Reports
Volume38
Issue number8
DOIs
Publication statusPublished - 01-11-2011

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Citrus
Bovine Serum Albumin
Thermodynamics
Flavonoids
Metals
Ions
Fluorescence
Proteins
Secondary Protein Structure
Fluorescence Resonance Energy Transfer
Fluorescence Polarization
Fluorescence Spectrometry
Circular Dichroism
Hydrogen
Buffers
Phosphates
hesperetin
Temperature

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Cite this

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abstract = "The mechanism of interaction of a non-glycosidic citrus flavonoid, hesperitin (HES) with bovine serum albumin (BSA) was studied by UV-vis absorption, fluorescence, FT-IR, circular dichroism, fluorescence anisotropy and synchronous fluorescence spectroscopy in phosphate buffer of pH 7.4. Fluorescence data revealed that the fluorescence quenching of BSA by HES was the result of the formed complex of HES-BSA. The binding constants and thermodynamic parameters at four different temperatures, the location of binding, and the nature of binding force were determined. The hydrogen bonds interactions were found to be the predominant intermolecular forces to stabilize the complex. The conformation of BSA was discussed by synchronous fluorescence and CD methods. The alterations of protein secondary structure upon complexation with HES were evident from the gradual decrease in a-helicity. The distance between the donor (BSA) and acceptor (flavonoid) was calculated from the fluorescence resonance energy transfer and found to be 1.978 nm. Common ions viz., Zn 2+, K +, Cu 2+, Ni 2+, Mn 2+ and Co 2+ were found to influence the binding of flavonoid to protein.",
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Evaluation of binding and thermodynamic characteristics of interactions between a citrus flavonoid hesperitin with protein and effects of metal ions on binding. / Hegde, Ashwini H.; Sandhya, B.; Seetharamappa, J.

In: Molecular Biology Reports, Vol. 38, No. 8, 01.11.2011, p. 4921-4929.

Research output: Contribution to journalArticle

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