Five Kinds Of Chinese Medicine Active Ingredients Of Three Myosin Interaction Research

Objective Five active components of Chinese herbs were selected as research targets, such as deoxyschizandrin, y-Schisandrin, rhein, emodin, chrysophanol. Three globulins (including human serum albumin, bovine serum albumin and lysozyme) were used as model proteins. Using spectroscopic methods and cyclic voltammetry, the interactions of five active components with three globulins had been investigated under simulative physiological condition.Methods The changes of the UV-vis absorbance, the electrochemical property and resonance light scattering signal before and after the interactions of deoxyschizandrin, y-Schisandrin with serum albumin (SA) and the interactions of rhein, emodin, chrysophanol with lysozyme (LYSO) were investigated by the utraviolet difference spectra, resonance light scattering (RLS) and cyclic voltammetry(CV). The parameters of the interaction between Chinese herb active components and three globulins were obtained by the fluorescence quenching titration, and the influence of six common metal ions such as Zn2+ on the interaction of deoxyschizandrin,γ-Schisandrin with SA and the influence of six rare earth ions such as Eu3+ on the interaction of rhein, emodin, chrysophanol with LYSO were studied also. The effects of Chinese herb active components on the conformation of SA and LYSO were investigated by synchronous fluorescence.Results The results of ultraviolet spectroscopy showed that the 1:1 compounds were formed between Chinese herb active components and metal ions. The binding of deoxyschizandrin,γ-Schisandrin and SA, rhein, emodin, chrysophanol and LYSO were demonstrated by the ultraviolet difference spectra, RLS and CV. The results of fluorescence spectrometry showed that the endogenous fluorescence of three globulins had been significantly quenched by Chinese herb active components, the mechanism of fluorescence quenching were static quenching with non-radiation energy transfer and the major driving force were hydrogen bond and Vander Waals. The binding parameters of deoxyschizandrin and SA were as follows:for BSA and HSA, the binding constants were 3.85×104and 6.42×103 L-moL-1; the numbers of binding sites were 0.944 and 0.993; the binding distances were 1.53 and 1.60 nm, respectively. The binding parameters ofγ-Schisandrin and SA were as follows:for BSA and HSA, the binding constants were 1.85×104 and 3.97×103 L·moL-1, the numbers of binding sites were 0.815 and 0.700, the binding distances were 1.65 and 2.18 nm, respectively. The binding parameters of rhein, emodin, chrysophanol and LYSO were as follows:the binding constants were 1.26×103,1.09×104 and 1.87×104 L·mol-1; the numbers of binding sites were 0.729,0.703 and 0.759; the binding distances were 3.83,2.82 and 2.55 nm, respectively. The results of synchronous fluorescence demonstrated that the binding site was closer to tryptophan residues and the hydrophobicity of tryptophan residues was decreased, but rhein had no effect on the transition of LYSO molecular conformation. In addition, the effect of metal ions on the binding of different drug-protein complexes was discussed comparatively.Conclusion The binding of deoxyschizandrin,γ-Schisandrin and SA, rhein, emodin, chrysophanol and LYSO were indicated by synchronous fluorescence, but rhein had no effect the transition of LYSO molecular conformation. The effect of commom metal ions (Zn2+, et al) and rare earth ions (Eu3+, et al) on the binding constants and the interaction force of different drug-protein complexes was discussed comparatively.