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Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods

Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods


Titill: Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods
Höfundur: Ma, Rui
Pan, Hong
Shen, Tao
Li, Peng
Chen, Yanan
Li, Zhenyu
Di, Xiaxia
Wang, Shuqi
Útgáfa: 2017-08-09
Tungumál: Enska
Umfang: 1317
Háskóli/Stofnun: Háskóli Íslands
University of Iceland
Svið: Heilbrigðisvísindasvið (HÍ)
School of Health Sciences (UI)
Deild: Lyfjafræðideild (HÍ)
Faculty of Pharmaceutical Sciences (UI)
Birtist í: Molecules;22(12)
ISSN: 1420-3049
DOI: 10.3390/molecules22081317
Efnisorð: Woodwardia unigemmata; Multidrug resistance; Doxorubicin-resistant K562/A02 cells; Bovine serum albumin; Molecular docking; Burknar; Lyfjafræði
URI: https://hdl.handle.net/20.500.11815/579

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Tilvitnun:

Ma, R., Pan, H., Shen, T., Li, P., Chen, Y., Li, Z., . . . Wang, S. (2017). Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods. Molecules, 22(8), 1317. doi:10.3390/molecules22081317

Útdráttur:

Phytochemical investigation on the methanol extract of Woodwardia unigemmata resulted in the isolation of seven flavonoids, including one new flavonol acylglycoside (1). The structures of these compounds were elucidated on the basis of extensive spectroscopic analysis and comparison of literature data. The multidrug resistance (MDR) reversing activity was evaluated for the isolated compounds using doxorubicin-resistant K562/A02 cells model. Compound 6 showed comparable MDR reversing effect to verapamil. Furthermore, the interaction between compounds and bovine serum albumin (BSA) was investigated by spectroscopic methods, including steady-state fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular docking approach. The experimental results indicated that the seven flavonoids bind to BSA by static quenching mechanisms. The negative ∆H and ∆S values indicated that van der Waals interactions and hydrogen bonds contributed in the binding of compounds 2–6 to BSA. In the case of compounds 1 and 7 systems, the hydrophobic interactions play a major role. The binding of compounds to BSA causes slight changes in the secondary structure of BSA. There are two binding sites of compound 6 on BSA and site I is the main site according to the molecular docking studies and the site marker competitive binding assay

Leyfi:

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. (CC BY 4.0).

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