Abstract
The interaction between dehydroeburicoic acid (DeEA), a triterpene purified from medicinal fungi and the major transport protein, human serum albumin (HSA), were systematically studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach under simulated physiological conditions. The intrinsic fluorescence of HSA was quenched through the combination of static and dynamic quenching mechanism. DeEA cannot be stored and carried by HSA in the body at higher temperature. The hydrogen bonding, hydrophobic force and van der Waals force were major acting forces. The site II was the major binding site. The energy transfer could occur with high probability and the binding distance was 3.29 nm. The binding process slightly changed the conformation and microenvironment of HSA. The DeEA molecule entered the hydrophobic cleft of HSA and formed the hydrogen bonding with Glu-492 and Lys-545.
Highlights
The results revealed that dehydroeburicoic acid (DeEA) could interact with human serum albumin (HSA) and the energy transfer could occur with high probability
The interaction between DeEA and HSA was systematically investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach
The fluorescence spectroscopy results suggested that DeEA quenched the intrinsic fluorescence of HSA through the combination of static and dynamic quenching mechanism
Summary
It can protect the liver from CCl4-induced oxidative stress and tissue injuries [3]. It possesses analgesic and anti-inflammatory effects [4] It exhibits antitumor activity against the human glioblastoma U87MG [2] [5]. Human serum albumin (HSA) is significant in the blood circulatory system. It contains 585 amino acid residues [8] [9]. Each domain contains two subdomains (IA, IB, IIA, IIB, IIIA and IIIB). It has two high-affinity binding sites (site I and site II) [11] [12].
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