Binding of curcumin with bovine serum albumin in the presence of ι-carrageenan and implications on the stability and antioxidant activity of curcumin

J Agric Food Chem. 2013 Jul 24;61(29):7150-5. doi: 10.1021/jf401827x. Epub 2013 Jul 12.

Abstract

This work studied the influences of formation of BSA/ι-carrageenan complexes on the binding, stability, and antioxidant activity of curcumin. In the presence of BSA and ι-carrageenan, curcumin gives higher intensities of absorption and fluorescence than free curcumin and curcumin only combined with BSA. The added ι-carrageenan is observed to promote curcumin for quenching the instrinsic fluorescence of BSA. These results are explained in terms of the formation of BSA/ι-carrageenan complexes, which help to stabilize the folded structure of BSA for providing curcumin with a more hydrophobic microenvironment. The small difference in anisotropy values of curcumin with BSA alone and of BSA/ι-carrageenan complexes suggests that ι-carrageenan acts as outer stretch conformation in BSA/ι-carrageenan complexes but does not directly disturb the hydrophobic pockets inside BSA, where curcumin is hydrophobically located. The determined values of the binding constant are higher for curcumin with BSA/ι-carrageenan complexes than with BSA alone. Moreover, BSA/ι-carrageenan complexes are found to be superior to single BSA for enhancing the stability and DPPH radical-scavenging ability of curcumin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrageenan / chemistry*
  • Curcumin / chemistry*
  • Curcumin / metabolism*
  • Curcumin / pharmacology
  • Drug Stability
  • Fluorescence
  • Fluorescence Polarization
  • Hydrogen-Ion Concentration
  • Hydrophobic and Hydrophilic Interactions
  • Serum Albumin, Bovine / chemistry
  • Serum Albumin, Bovine / metabolism*

Substances

  • Serum Albumin, Bovine
  • Carrageenan
  • Curcumin