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Int. J. Mol. Sci. 2013, 14(7), 14185-14203; doi:10.3390/ijms140714185
Article

Characterization of the Interaction between Eupatorin and Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods

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Received: 26 February 2013 / Revised: 20 May 2013 / Accepted: 27 June 2013 / Published: 9 July 2013
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Abstract

This study investigated the interaction between eupatorin and bovine serum albumin (BSA) using ultraviolet-visible (UV-vis) absorption, fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular modeling at pH 7.4. Results of UV-vis and fluorescence spectroscopies illustrated that BSA fluorescence was quenched by eupatorin via a static quenching mechanism. Thermodynamic parameters revealed that hydrophobic and electrostatic interactions played major roles in the interaction. Moreover, the efficiency of energy transfer, and the distance between BSA and acceptor eupatorin, were calculated. The effects of eupatorin on the BSA conformation were analyzed using UV-vis, CD, and synchronous fluorescence. Finally, the binding of eupatorin to BSA was modeled using the molecular docking method.
Keywords: eupatorin; bovine serum albumin; binding; spectroscopy; molecular modeling eupatorin; bovine serum albumin; binding; spectroscopy; molecular modeling
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Xu, H.; Yao, N.; Xu, H.; Wang, T.; Li, G.; Li, Z. Characterization of the Interaction between Eupatorin and Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods. Int. J. Mol. Sci. 2013, 14, 14185-14203.

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