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Abstract
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Curcumin has multiple pharmacological effects, but it has poor stability. Complexation of
curcumin with metals improves its stability. Here, the effects of vanadyl curcumin and vanadyl
diacetylcurcumin on the function and structure of horseradish peroxidase enzyme were
evaluated by spectroscopic techniques. Cytotoxic effect of the complexes was also assessed on
MCF-7 breast cancer, bladder and LNCaP prostate carcinoma cell line. The results showed that
the complexes improve catalytic activity of HRP, and also increase its tolerance against the
oxidative condition. The result also indicated that the affinity of HRP for hydrogen peroxide
substrate decreases, while the affinity increases for phenol substrate. Circular dichroism and
fluorescence spectroscopies showed that compactness of the enzyme structure around the
catalytic heme group and the distance between the heme group and tryptophan residue
decreases after the binding. The antibacterial and cytotoxic results indicated that the
complexes have anticancer potential, but they have no considerable antibacterial activity
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