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 Scijournal_title
International journal of molecular sciencesauthors
Xu H,Yao N,Xu H,Wang T,Li G,Li Zdoi
10.3390/ijms140714185subject
Has Abstractpub_date
2013-07-09 00:00:00pages
14185-203issue
7issn
1422-0067pii
ijms140714185journal_volume
14pub_type
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