Circular dichroism and fluorescence spectroscopic study on the interaction of bisdemethoxycurcumin and diacetylbisdemethoxycurcumin with human serum albumin

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Abstract

The interactions of bisdemethoxycurcumin (BDMC) as a bioactive constituent of turmeric and diacetylbisdemethoxycurcumin (DABC) as a novel synthetic derivative of curcumin with human serum albumin (HSA) have been investigated by fluorescence and circular dichroism (CD) spectroscopy. The binding parameters, including the number of substantive binding sites and the binding constants, have been estimated from the analysis of fluorescence measurements. The estimated binding parameters indicated that BDMC has higher affinity than DABC to bind HSA, suggesting the essential role of the phenolic OH groups of BDMC, which are acetylated in DABC. It was found that the binding site for BDMC and DABC is located in the vicinity of Trp-214 in subdomain IIA, which is the same as binding site for curcumin (CUR). The minor changes on the far-UV circular dichroism spectra resulted in partial changes in the calculated secondary structure contents of HSA. The negligible alteration in the secondary structure of HSA indicated that ligand-induced conformational changes are localized in the binding site and do not involve considerable changes in the protein folding. The visible CD spectra indicated that the optical activity observed during the ligand binding is due to induced-protein chirality.

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