Binding mechanism of lipase to Ligupurpuroside B extracted from Ku-Ding tea as studied by multi-spectroscopic and molecular docking methods

The interaction of lipase with Ligupurpuroside B was studied by multiple spectroscopic techniques, enzyme activity and molecular modeling under simulative physiological condition. According to Stern-Volmer equation, fluorescence of lipase was quenched by Ligupurpuroside B via a static quenching mech...

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Veröffentlicht in:	International journal of biological macromolecules 2018-12, Vol.120 (Pt B), p.1345-1352
Hauptverfasser:	Ying, Ming, Meti, Manjunath D., Xu, Hong, Wang, Yuhan, Lin, Jialiang, Wu, Zhibing, Han, Qingguo, Xu, Xu, He, Zhendan, Hong, Wenxu, Hu, Zhangli
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Enzyme activity Hydrophobic and Hydrophilic Interactions Ligupurpuroside B Lipase Lipase - chemistry Lipase - metabolism Molecular docking Molecular Docking Simulation Protein Binding Protein Conformation Spectrum Analysis Tea - chemistry Thermodynamics
Online-Zugang:	Volltext
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