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
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container_end_page 1352
container_issue Pt B
container_start_page 1345
container_title International journal of biological macromolecules
container_volume 120
creator Ying, Ming
Meti, Manjunath D.
Xu, Hong
Wang, Yuhan
Lin, Jialiang
Wu, Zhibing
Han, Qingguo
Xu, Xu
He, Zhendan
Hong, Wenxu
Hu, Zhangli
description 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 mechanism because of formation of Ligupurpuroside B-lipase complex. Binding constants, number of binding sites & thermodynamic parameters were evaluated. The values of ΔGo (−25.085 kJ mol−1), ΔHo (−12.14 kJ mol−1) and ΔSo (+43.45 J mol−1 K−1) at 298 K indicated that Ligupurpuroside B-lipase interaction is spontaneous and hydrophobic interaction is the main force stabilizing the Ligupurpuroside B-lipase complex. The enzyme activity assay showed that Ligupurpuroside B inhibited lipase activity efficiently. Synchronous fluorescence spectra (SFS) suggested that Ligupurpuroside B is closer to Trp residues than to Tyr residues. All above experimental results were confirmed by molecular docking studies, which further indicated the binding site of Ligupurpuroside B on the surface of lipase, and the amino acid residues of lipase interacting with Ligupurpuroside B. Our present research work gives valuable information on the design of drugs with lipase as a carrier and should be useful for food industries. •Ligupurpuroside B effectively quenched the intrinsic fluorescence of lipase by static quenching mechanism.•Thermodynamic parameter were calculated to explain the week interactions between ligupurpuroside B and lipase.•The number of binding sites closed to unity indicating a single class of binding of ligupurpuroside B to lipase.•The enzyme activity results suggested that Ligupurpuroside B can inhibit lipase activity.•Molecular docking study presented the binding site of Ligupurpuroside B on lipase and the amino acid residues involved.
doi_str_mv 10.1016/j.ijbiomac.2018.09.086
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According to Stern-Volmer equation, fluorescence of lipase was quenched by Ligupurpuroside B via a static quenching mechanism because of formation of Ligupurpuroside B-lipase complex. Binding constants, number of binding sites &amp; thermodynamic parameters were evaluated. The values of ΔGo (−25.085 kJ mol−1), ΔHo (−12.14 kJ mol−1) and ΔSo (+43.45 J mol−1 K−1) at 298 K indicated that Ligupurpuroside B-lipase interaction is spontaneous and hydrophobic interaction is the main force stabilizing the Ligupurpuroside B-lipase complex. The enzyme activity assay showed that Ligupurpuroside B inhibited lipase activity efficiently. Synchronous fluorescence spectra (SFS) suggested that Ligupurpuroside B is closer to Trp residues than to Tyr residues. All above experimental results were confirmed by molecular docking studies, which further indicated the binding site of Ligupurpuroside B on the surface of lipase, and the amino acid residues of lipase interacting with Ligupurpuroside B. 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Our present research work gives valuable information on the design of drugs with lipase as a carrier and should be useful for food industries. •Ligupurpuroside B effectively quenched the intrinsic fluorescence of lipase by static quenching mechanism.•Thermodynamic parameter were calculated to explain the week interactions between ligupurpuroside B and lipase.•The number of binding sites closed to unity indicating a single class of binding of ligupurpuroside B to lipase.•The enzyme activity results suggested that Ligupurpuroside B can inhibit lipase activity.•Molecular docking study presented the binding site of Ligupurpuroside B on lipase and the amino acid residues involved.</description><subject>Binding Sites</subject><subject>Enzyme activity</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Ligupurpuroside B</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Lipase - metabolism</subject><subject>Molecular docking</subject><subject>Molecular Docking Simulation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Spectrum Analysis</subject><subject>Tea - chemistry</subject><subject>Thermodynamics</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctuFDEQRS0EIkPgFyIv2XTHj37YO0jCS4zEBtaW265OPLTbjR8R-QZ-Go8mYYtkqSTXuXVVdRG6oKSlhA6Xh9YdJhe8Ni0jVLREtkQMz9COilE2hBD-HO0I7WgjKCdn6FVKh_o79FS8RGecMMZJ3-3Qnyu3WrfeYg_mTq8ueRxmvLhNJ8A54L27LVuJ9YXkLOArDL9z1CaDxXMMHn8tzc1Rn0FjnXDKxbramx6wL0t2TdrA5Co2YXMG69ViHxYwZdER22B-nrzzXbDpNXox6yXBm8d6jn58_PD9-nOz__bpy_X7fWP4IHJDqen7UQjNjQDD9cSs5KPumWVakHmYpYSOjL3suZnmkQPryNBVpht5L9nAz9Hb09wthl8FUlbeJQPLolcIJSlGieS8590RHU6oqSukCLPaovM6PihK1DEIdVBPQahjEIpIVYOowotHjzJ5sP9kT5evwLsTAHXTewdRJeNgNWBdrBdTNrj_efwFfHaeuQ</recordid><startdate>201812</startdate><enddate>201812</enddate><creator>Ying, Ming</creator><creator>Meti, Manjunath D.</creator><creator>Xu, Hong</creator><creator>Wang, Yuhan</creator><creator>Lin, Jialiang</creator><creator>Wu, Zhibing</creator><creator>Han, Qingguo</creator><creator>Xu, Xu</creator><creator>He, Zhendan</creator><creator>Hong, Wenxu</creator><creator>Hu, Zhangli</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201812</creationdate><title>Binding mechanism of lipase to Ligupurpuroside B extracted from Ku-Ding tea as studied by multi-spectroscopic and molecular docking methods</title><author>Ying, Ming ; 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According to Stern-Volmer equation, fluorescence of lipase was quenched by Ligupurpuroside B via a static quenching mechanism because of formation of Ligupurpuroside B-lipase complex. Binding constants, number of binding sites &amp; thermodynamic parameters were evaluated. The values of ΔGo (−25.085 kJ mol−1), ΔHo (−12.14 kJ mol−1) and ΔSo (+43.45 J mol−1 K−1) at 298 K indicated that Ligupurpuroside B-lipase interaction is spontaneous and hydrophobic interaction is the main force stabilizing the Ligupurpuroside B-lipase complex. The enzyme activity assay showed that Ligupurpuroside B inhibited lipase activity efficiently. Synchronous fluorescence spectra (SFS) suggested that Ligupurpuroside B is closer to Trp residues than to Tyr residues. All above experimental results were confirmed by molecular docking studies, which further indicated the binding site of Ligupurpuroside B on the surface of lipase, and the amino acid residues of lipase interacting with Ligupurpuroside B. Our present research work gives valuable information on the design of drugs with lipase as a carrier and should be useful for food industries. •Ligupurpuroside B effectively quenched the intrinsic fluorescence of lipase by static quenching mechanism.•Thermodynamic parameter were calculated to explain the week interactions between ligupurpuroside B and lipase.•The number of binding sites closed to unity indicating a single class of binding of ligupurpuroside B to lipase.•The enzyme activity results suggested that Ligupurpuroside B can inhibit lipase activity.•Molecular docking study presented the binding site of Ligupurpuroside B on lipase and the amino acid residues involved.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>30223054</pmid><doi>10.1016/j.ijbiomac.2018.09.086</doi><tpages>8</tpages></addata></record>
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subjects 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
title Binding mechanism of lipase to Ligupurpuroside B extracted from Ku-Ding tea as studied by multi-spectroscopic and molecular docking methods
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