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Synthesis of Morin–Zinc(II) Complex and its Interaction with Serum Albumin

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Abstract

A morin–zinc(II) complex (MZ) was synthesized and its interaction with bovine serum albumin (BSA) were studied by molecular spectroscopy including fluorescence emission spectra, UV-visible spectra, circular dichroism (CD) spectra, three-dimensional fluorescence spectra, and synchronous fluorescence spectra. The interaction mechanism of BSA and MZ was discussed by fluorescence quenching method and Förster non-radiation energy transfer theory. The thermodynamic parameters ΔH θ, ΔG θ, ΔS θ at different temperatures were calculated and the results indicate the interaction is an exothermic as well as entropy-driven process. Hydrogen bond forces played the most important role in the reaction. The fluorescence probe experiment showed that the binding site of MZ is in subdomain IIA of BSA and the distance between BSA and MZ is 3.17 nm at normal body temperature. The conformation changes of BSA in presence of MZ were investigated by CD spectra and three-dimensional fluorescence spectra.

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Acknowledgments

The authors gratefully acknowledge the fund support of Science and Technology Research Program of the Education Department, Hubei, China (Grant No. B20104301) and Scientific Research Project of Jingchu University of Technology (Grant No. ZR200905).

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Authors and Affiliations

  1. College of Chemical and Environmental Engineering, Yangtze University, Jingzhou, Hubei, 434023, People’s Republic of China

    Hua-xin Zhang & Ping Mei

  2. College of Chemical and Pharmaceutical Engineering, Jingchu University of Technology, Jingmen, Hubei, 448000, People’s Republic of China

    Hua-xin Zhang

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  1. Hua-xin Zhang
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  2. Ping Mei
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Correspondence to Ping Mei.

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Zhang, Hx., Mei, P. Synthesis of Morin–Zinc(II) Complex and its Interaction with Serum Albumin. Biol Trace Elem Res 143, 677–687 (2011). https://doi.org/10.1007/s12011-010-8903-y

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  • DOI: https://doi.org/10.1007/s12011-010-8903-y

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