Abstract
The interaction of HE–Eu(III) complex (HE = hematoxylin) with Herring-sperm DNA (hsDNA) has been studied by absorption spectra, fluorescence, and viscosity measurements in physiological buffer (pH = 7.40). The binding constant of HE–Eu(III) complex to hsDNA was obtained by double reciprocal method at 298 and 310 K and the corresponding thermodynamic parameters (Δr Hm⊖ = 8.55 × 104 J mol−1, Δr Gm⊖ = −3.01 × 104 J mol−1, Δr Sm⊖ = 387.95 J mol−1 K−1) were calculated, showing that the interaction between HE–Eu(III) complex and hsDNA was driven mainly by entropy. The value of K indicated that the binding mode of HE–Eu(III) complex with DNA was not classical intercalation. These results were further supported by viscosity method and competitive binding experiment. Scatchard analysis suggests that the interaction mode was a mixed binding, which contains partial intercalation and groove binding.
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