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ABSTRACT
The binding mechanism of Hematoxylin-Zn(II) complex with Herring sperm DNA has been investigated using UV–vis and fluorescence spectroscopies and viscosity measurement. With the increase in the concentration of complex, the viscosity of DNA decreased, and the binding mode is more detailed: there is partially intercalate binding. Furthermore, besides the intercalate binding, the existence of groove binding was confirmed through the ionic strength experiment in Scatchard analysis. Thermodynamic studies provided some thermodynamic parameters: ΔrHmΘ = 1.43 × 105 J mol−1, ΔrSmΘ = 576.14 J mol−1, ΔrGmΘ303K = −3.16 × 104 J mol−1, they illustrated that the binding mechanism between HE-Zn(II) complex and hsDNA was driven mainly by entropy.
Acknowledgment
The authors are grateful for the apparatus support of the Analytical and Testing Center of Sichuan Normal University.
Funding
This work was supported by the National Natural Science Foundation of China under Grant No. 30572254 and Key Fund Project of Sichuan Provincial Department of Education (NO. 14ZA0027).