Angelica sinensis(Oliv.) Diels combined treatment with warfarin would increase the risk of bleeding. Ferulic acid is an abundant hydroxycinnamic acid inA. sinensisand warfarin is the most widely used oral anticoagulant. The studies on supermolecular interaction of warfarin with human serum albumin (HSA) and the influence of ferulic acid on the binding would contribute to the understanding of the metabolic processes of warfarin and the effect of ferulic acid. We focus on investigating the effect of warfarin on fluorescence spectrum of human serum albumin (HSA), fluorescence quenching mechanism, binding constant, Hill coefficient, binding mode, and the effect of different ferulic acid concentrations on the binding. Warfarin quenched the intrinsic fluorescence of HSA mainly by static quenching. Accession of ferulic acid reduced the binding of HSA-warfarin. By decreasing binding constant and the Hill coefficient of warfarin with HSA, ferulic acid could improve the plasma concentration of free warfarin, which would increase the risk of bleeding. Warfarin’s free concentration increased at least 50% under the condition of simulated human body. The results indicated thatA. sinensiscombined treatment with warfarin would increase the risk of bleeding. And the results provide an important theoretical support for warfarin used as oral anticoagulant.
The interaction of hyperoside (Hyp) with human serum albumin (HSA) and effect of glucose on the binding were studied in simulating physiological condition (pH 7.40). The results suggested that Hyp quenched the endogenous fluorescence of HSA via a static quenching process with the distance of 1.95 nm between Hyp and HSA. Hydrophobic forces played a major role in stabilizing the Hyp-HSA complex. Through synchronous fluorescence monitoring of conformation of HSA, we found that the binding to Hyp can change the microenvironment around tryptophan (Trp) residues. Increasing in glucose concentration over a range from 0 to 9 mM decreased the binding ability of HSA to Hyp, implying that increasing in glucose concentration would increase the concentration of free Hyp.
The changes of lysozyme conformation in the absence and presence of luteolin and luteoloside were investigated by spectral analysis including fluorescence, UV, CD, Raman, and ATR-FTIR, and the biological activity of lysozyme was investigated by lysozyme assay kit. The results showed that the microenvironment hydrophobicity of lysozyme increased and peptide extension decreased with the addition of luteolin or luteoloside. The α-helix of lysozyme might be influenced by luteolin or luteoloside, and its relative content had a significant difference after adding luteolin or luteoloside by the ATR-FTIR method, which was reconfirmed by CD and Raman spectra. The lysozyme activity changed obviously after adding luteolin or luteoloside. All of the conclusions above indicated the active site of lysozyme in the α-helix might be influenced by luteolin and luteoloside.
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