Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
11026028 | International Journal of Biological Macromolecules | 2018 | 37 Pages |
Abstract
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 ÎGo (â25.085â¯kJâ¯molâ1), ÎHo (â12.14â¯kJâ¯molâ1) and ÎSo (+43.45â¯Jâ¯molâ1â¯Kâ1) at 298â¯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.
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Authors
Ming Ying, Manjunath D. Meti, Hong Xu, Yuhan Wang, Jialiang Lin, Zhibing Wu, Qingguo Han, Xu Xu, Zhendan He, Wenxu Hong, Zhangli Hu,