Investigations to reveal the nature of interactions of human hemoglobin with curcumin using optical techniques

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

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Curcumin (CUR) is an important bioactive compound present in the rhizome of Curcuma longa. Herein, we report the interaction of CUR with human hemoglobin (Hb) using various biophysical methods viz., fluorescence, UV absorption, resonance light scattering spectra (RLS), synchronous fluorescence, fluorescence anisotropy, circular dichroism (CD) and three-dimensional fluorescence. There was a considerable quenching of the intrinsic fluorescence of Hb upon binding to CUR through dynamic quenching mechanism. The distance (r) between the donor and acceptor was obtained from the Forster's theory of fluorescence resonance energy transfer (FRET) and found to be 1.55. nm. Alterations in the conformation of Hb due to its interaction with CUR were confirmed by UV absorption and CD spectroscopic methods. The α-helicity of Hb was found to decrease upon binding with CUR.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalInternational Journal of Biological Macromolecules
Volume52
Issue number1
DOIs
Publication statusPublished - 01-01-2013

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Curcumin
Hemoglobins
Fluorescence
Circular Dichroism
Quenching
Curcuma
Fluorescence Resonance Energy Transfer
Rhizome
Fluorescence Polarization
Light scattering
Conformations
Anisotropy
Light

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Cite this

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abstract = "Curcumin (CUR) is an important bioactive compound present in the rhizome of Curcuma longa. Herein, we report the interaction of CUR with human hemoglobin (Hb) using various biophysical methods viz., fluorescence, UV absorption, resonance light scattering spectra (RLS), synchronous fluorescence, fluorescence anisotropy, circular dichroism (CD) and three-dimensional fluorescence. There was a considerable quenching of the intrinsic fluorescence of Hb upon binding to CUR through dynamic quenching mechanism. The distance (r) between the donor and acceptor was obtained from the Forster's theory of fluorescence resonance energy transfer (FRET) and found to be 1.55. nm. Alterations in the conformation of Hb due to its interaction with CUR were confirmed by UV absorption and CD spectroscopic methods. The α-helicity of Hb was found to decrease upon binding with CUR.",
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Investigations to reveal the nature of interactions of human hemoglobin with curcumin using optical techniques. / Hegde, Ashwini H.; Sandhya, B.; Seetharamappa, J.

In: International Journal of Biological Macromolecules, Vol. 52, No. 1, 01.01.2013, p. 133-138.

Research output: Contribution to journalArticle

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