The interaction between dehydroeburicoic acid (DeEA), a triterpene purified\nfrom medicinal fungi and the major transport protein, human serum albumin\n(HSA), were systematically studied by fluorescence spectroscopy, synchronous\nfluorescence spectroscopy, three-dimensional fluorescence spectroscopy\nand molecular docking approach under simulated physiological conditions.\nThe intrinsic fluorescence of HSA was quenched through the combination of\nstatic and dynamic quenching mechanism. DeEA cannot be stored and carried\nby HSA in the body at higher temperature. The hydrogen bonding, hydrophobic\nforce and van der Waals force were major acting forces. The site II\nwas the major binding site. The energy transfer could occur with high probability\nand the binding distance was 3.29 nm. The binding process slightly\nchanged the conformation and microenvironment of HSA. The DeEA molecule\nentered the hydrophobic cleft of HSA and formed the hydrogen bonding\nwith Glu-492 and Lys-545.
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