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Int J Mol Sci. 2013 Jul 9;14(7):14185-203. doi: 10.3390/ijms140714185.

Characterization of the interaction between eupatorin and bovine serum albumin by spectroscopic and molecular modeling methods.

Author information

1
Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, China. lzq@jlu.edu.cn.

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.

PMID:
23839090
PMCID:
PMC3742238
DOI:
10.3390/ijms140714185
[Indexed for MEDLINE]
Free PMC Article
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