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1 June 2003 Photophysical Studies on Binding of Curcumin to Bovine Serum Albumin
A. Barik, K. I. Priyadarsini, Hari Mohan
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The excited-state photophysical properties of curcumin in the presence of bovine serum albumin (BSA) have been studied. The absorption and fluorescence changes in curcumin on binding to BSA have been followed at varying concentrations of either curcumin or BSA to determine the binding constant, which has been found to be ∼104 to 105 M−1. Stopped-flow kinetics studies suggested at least two distinct kinetic steps for the binding of curcumin to BSA. The photophysical properties of the singlet-excited state of the curcumin–BSA complex have also been studied. Whereas the absorption spectrum of curcumin is redshifted, the fluorescence spectrum of curcumin was blueshifted in the presence of BSA. The fluorescence quantum yield of curcumin on complexing with BSA was ∼0.05. Steady-state fluorescence anisotropy studies showed a significant increase in the anisotropy value of 0.37 in BSA-bound curcumin. The fluorescence decay of the curcumin–BSA complex followed a biexponential decay with fluorescence lifetimes of 413 ps (33%) and 120 ps (67%). On the basis of these complementary results, it has been concluded that curcumin shows very high binding to BSA, probably at the hydrophobic cavities inside the protein.

A. Barik, K. I. Priyadarsini, and Hari Mohan "Photophysical Studies on Binding of Curcumin to Bovine Serum Albumin," Photochemistry and Photobiology 77(6), 597-603, (1 June 2003).<0597:PSOBOC>2.0.CO;2
Received: 20 January 2003; Accepted: 1 March 2003; Published: 1 June 2003

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