The Protein Journal

, Volume 28, Issue 3–4, pp 117–123

Interaction of Curcumin and Diacetylcurcumin with the Lipocalin Member β-Lactoglobulin

  • Fakhrossadat Mohammadi
  • Abdol-Khalegh Bordbar
  • Adeleh Divsalar
  • Khosro Mohammadi
  • Ali Akbar Saboury


The binding of curcumin (CUR) and diacetylcurcumin (DAC) to bovine beta-lactoglobulin (BLG) genetic variant B was investigated by fluorescence and circular dichroism techniques. The binding parameters including number of substantive binding sites and the binding constants have been evaluated by fluorescence quenching method. The distance (r) between donor (BLG) and acceptor (CUR and DAC) was obtained according to the Förster’s theory of non-radiative energy transfer. The far-UV circular dichroism spectra were used to investigate the possible changes in the secondary structure of BLG in the presence of CUR and DAC and showed that these two ligands change the α-helix and random coil contents of this protein to some extent. The visible circular dichroism spectra indicated that the optical activity during the ligand binding was observed due to the induced-protein chirality. All of the achieved results suggested the important role of the phenolic OH group of CUR in the binding process resulted in more affinity of CUR than DAC for binding to BLG.


Curcumin Diacetylcurcumin Bovine β-lactoglobulin Fluorescence Circular dichroism 









Circular dichroism


Aspartic acid








Human serum albumin


Bovine serum albumin


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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Fakhrossadat Mohammadi
    • 1
  • Abdol-Khalegh Bordbar
    • 1
  • Adeleh Divsalar
    • 2
  • Khosro Mohammadi
    • 3
  • Ali Akbar Saboury
    • 2
  1. 1.Laboratory of Biophysical Chemistry, Department of ChemistryUniversity of IsfahanIsfahanIran
  2. 2.Institute of Biochemistry and BiophysicsUniversity of TehranTehranIran
  3. 3.Department of Chemistry, College of SciencesPersian Gulf UniversityBushehrIran

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