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应用多种色谱技术从华中五味子中分离纯化出一个稀有降三萜成分schicagenin A,采用荧光淬灭技术和紫外光谱方法研究该化合物与人血清白蛋白的相互作用机制,两者的相互作用研究显示:静态淬灭机制参与其中,提示schicagenin A与人血清白蛋白结合形成了复合物;在schicagenin A与人血清白蛋白的结合过程中疏水作用起了主要驱动作用;人血清白蛋白的ⅡA亚域(位点I)是schicagenin A与之的结合位点.本研究为schicagenin A在人体内进一步的生物活性研究和基于该化合物的新药设计提供了参考数据.
A variety of chromatographic techniques were used to separate and purify schickagenin A, a rare triterpenoid from Schisandra chinensis. The interaction mechanism between the compound and human serum albumin was studied by fluorescence quenching and UV spectroscopy. The interaction between the two : Static quenching mechanism involved, suggesting that schicagenin A and human serum albumin to form a complex; schicagenin A and human serum albumin binding process played a major role in the hydrophobic interaction; human serum albumin Ⅱ A sub-domain (Site I) is the binding site for schicagenin A. This study provides further data on the biological activity of schicagenin A in humans and the design of new drugs based on the compound.