JOURNAL OF LUMINESCENCE
·
2014
·
IF 2.367
Liang-liang Shen,Hong Xu,Feng-wen Huang,Yi Li,Jie Xiao,Hua-feng Xiao,Ming Ying,Sheng-li Tian,Zhen Yang,Gang Liu,Zhang-li Hu,Zhen-dan He,Kai Zhou
The interaction of Ligupurpuroside A with bovine serum albumin (BSA) has been investigated by fluorescence spectra , UV–vis absorption spectra , three-dimensional (3D) fluorescence spectra, synchronous fluorescence spectra and circular dichroism (CD) spectra along with a molecular docking method. The fluorescence experiments indicate that Ligupurpuroside A can quench the intrinsic fluorescence of BSA through a combined quenching way at the low concentration of Ligupurpuroside A, and a static quenching procedure at the high concentration. The thermodynamic analysis suggests that hydrogen bonds and van der Waals forces are the main forces between BSA and Ligupurpuroside A. According to the theory of Förster׳s non-radiation energy transfer, the binding distance between BSA and Ligupurpuroside A was calculated to be 2.73 nm, which implies that energy transfer occurs between BSA and Ligupurpuroside A. All these experimental results have been validated by the protein–ligand docking studies which show that Ligupurpuroside A binds to the residues located in the hydrophobic cavity on subdomain IIA of BSA. In addition, conformation change of BSA was observed from three-dimensional fluorescence spectra, synchronous fluorescence spectra and circular dichroism spectra under experimental conditions.
研究领域:
生物化学
·
药物化学
·
光谱学
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产品关联
DOI
高影响因子
Food Biophysics
·
2016
·Vol. 12
·期 1
·78-87
·
IF 1.605
Wu Zhibing,Shen Liangliang,Han Qingguo,Lu Jun,Tang Haifeng,Xu Xu,Xu Hong,Huang Fengwen,Xie Jiangfeng,He Zhendan,Zeng Zheling,Hu Zhangli
Ligupurpuroside A is a glycoside extracted from Ku-Ding tea. As extracts from Ku-Ding tea exhibit anti-inflammatory property, we hypothesize that Ligupurpuroside A may be an active compound which inhibits trypsin activity during the anti-inflammatory process. The mechanism and nature of inhibition of trypsin by Ligupurpuroside A have been studied by multi-spectroscopic method, enzyme-activity assay and molecular docking. Enzyme activity assay reveals that Ligupurpuroside A significantly inhibits the activity of trypsin through a competitive manner with an IC 50 value of 3.08 × 10 −3 mol L −1 . Fluorescence titration together with thermodynamic analysis indicate that a Ligupurpuroside A-trypsin complex is formed, and that hydrophobic force and hydrogen bonding are the main forces stabilizing the complex. UV-vis absorption, synchronous fluorescence and circular dichroism spectra show that the interaction between Ligupurpuroside A and trypsin induces conformational changes of trypsin with a decrease in the contents of α-helix and β-sheet. Finally, molecular docking further suggests that Ligupurpuroside A molecule binds within the active pocket of trypsin via hydrophobic force and hydrogen bond. Results from this study of the interaction of trypsin with its natural inhibitor should be useful to minimize the antinutritional effects and make full use of tea extracts in the food industry, and be also helpful to the design of the drugs for the diseases related to overexpression of trypsin.
研究领域:
生物化学
·
药物设计
·
食品科学
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DOI
高影响因子
MEDICINAL CHEMISTRY RESEARCH
·
2018
·Vol. 27
·期 7
·1822-1833
·
IF 1.607
Fan Yu,Xu Yang,Han Qing-Guo,Shen Liang-Liang,Xu Hong,Wu Zhi-Bing,Xu Xu,Ying Ming,He Zhen-Dan,Hu Zhang-Li
Enzyme-activity essay demonstrated that Ligupurpuroside A acts as a natural inhibitor of lipase in a competitive manner. The inhibition mechanism and nature of lipase by Ligupurpuroside A were investigated by fluorescence spectra, UV–Vis absorption spectra, circular dichroism (CD) spectra and molecular docking methods. Fluorescence experiments indicated that Ligupurpuroside A can quench the intrinsic fluorescence of lipase through a static quenching procedure. Thermodynamic analysis suggested that hydrophobic interaction is the main force between lipase and Ligupurpuroside A. Fluorescence resonance energy transfer experiment showed that an energy transfer from lipase to Ligupurpuroside A occurs with great possibility, confirming the presence of static quenching mechanism of lipase fluorescence by Ligupurpuroside A. Interestingly, conformation of lipase remained almost the same after bound to Ligupurpuroside A based on CD spectral experiments. All these experimental results were validated by the protein-ligand docking studies which further showed that Ligupurpuroside A could bind to the amino acid residues of the hydrophobic cavity on catalytic sites of lipase. This study should be helpful for the design of diet drug and the full use of Ligupurpuroside A in food industry.
研究领域:
生物化学
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药理学
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食品科学
·
分子生物学
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产品关联
DOI
高影响因子
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
·
2014
·
IF 2.129
Liangliang Shen,Hong Xu,Fengwen Huang,Yi Li,Huafeng Xiao,Zhen Yang,Zhangli Hu,Zhendan He,Zheling Zeng,Yinong Li
Ligupurpuroside A is one of the major glycoside in Ku-Din-Cha, a type of Chinese functional tea. In order to better understand its digestion and metabolism in humans, the interaction between Ligupurpuroside A and pepsin has been investigated by fluorescence spectra, UV–vis absorption spectra and synchronous fluorescence spectra along with molecular docking method. The fluorescence experiments indicate that Ligupurpuroside A can effectively quench the intrinsic fluorescence of pepsin through a combined quenching way at the low concentration of Ligupurpuroside A, and a static quenching procedure at the high concentration. The binding constant, binding sites of Ligupurpuroside A with pepsin have been calculated. The thermodynamic analysis suggests that non-covalent reactions, including electrostatic force, hydrophobic interaction and hydrogen bond are the main forces stabilizing the complex. According to the Förster’s non-radiation energy transfer theory, the binding distance between pepsin and Ligupurpuroside A was calculated to be 3.15 nm, which implies that energy transfer occurs between pepsin and Ligupurpuroside A. Conformation change of pepsin was observed from UV–vis absorption spectra and synchronous fluorescence spectra under experimental conditions. In addition, all these experimental results have been validated by the protein-ligand docking studies which show that Ligupurpuroside A is located in the cleft between the domains of pepsin.
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DOI
高影响因子
危险品化学品经营许可证（带存储）