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- W2361323666 abstract "Intrinsic fluorescence,absorption spectroscopy and the molecular modeling techniques were used to characterize piperine to human serum albumin(HSA).The synchronous fluorescence and absorption spectroscopes indicated that piperine participated in the microenvironment surrounding HSA in aqueous solution.Fluorescent displacement measurements confirmed that piperine bind HSA on site Ⅱ.The binding constants and the number of binding sites between piperine and HSA at different temperatures(300 K,310 K and 318 K) were calculated according to the data obtained from fluorescence titration.The molecular docking to reveal the possible binding mode suggested that the binding of piperine to HSA has appeared to be strong by a hydrophobic interaction and there are three hydrogen bonds interactions between the drug and the residues Arg 257,Arg222 and Arg218.The values of different thermodynamic parameters obtained from experimental data(the enthalpy change and the entropy change were calculated to be 33.11 kJ·mol 原1 and 18.90 J·mol 原1 ·K 原1) suggested that thhyed rcoogmenp lebxo.nds and vander Waals force interaction are the predominant intermolecular forces stabilizing" @default.
- W2361323666 created "2016-06-24" @default.
- W2361323666 creator A5063371558 @default.
- W2361323666 date "2010-01-01" @default.
- W2361323666 modified "2023-09-23" @default.
- W2361323666 title "Characterization of Piperine Binding Site on Human Serum Albumin" @default.
- W2361323666 hasPublicationYear "2010" @default.
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