期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 14, 期 7, 页码 14185-14203出版社
MDPI
DOI: 10.3390/ijms140714185
关键词
eupatorin; bovine serum albumin; binding; spectroscopy; molecular modeling
资金
- Key Laboratory for Molecular Enzymology and Engineering, the Ministry of Education, Jilin University
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.
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