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 1.55nm. 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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