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

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.

journal_name

Int J Mol Sci

authors

Xu H,Yao N,Xu H,Wang T,Li G,Li Z

doi

10.3390/ijms140714185

subject

Has Abstract

pub_date

2013-07-09 00:00:00

pages

14185-203

issue

7

issn

1422-0067

pii

ijms140714185

journal_volume

14

pub_type

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