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灯盏乙素与牛血清白蛋白相互作用的研究
引用本文:王丽,张爱平,杨锦艳,杨斌盛. 灯盏乙素与牛血清白蛋白相互作用的研究[J]. 中国药物与临床, 2007, 7(9): 667-669
作者姓名:王丽  张爱平  杨锦艳  杨斌盛
作者单位:1. 山西医科大学药物分析教研室,太原,030001
2. 山西大学分子科学研究所
摘    要:目的采用荧光、紫外光谱法研究在模拟人体生理条件下灯盏乙素与牛血清白蛋白(BSA)之间的相互作用。方法将灯盏乙素对牛血清白蛋白进行荧光淬灭滴定,利用Scatchard模型和F"rster非辐射能量转移理论得出灯盏乙素和牛血清白蛋白的结合参数。结果灯盏乙素与BSA的结合常数K=1.240×106,结合距离r=2.94nm,相互作用力主要为疏水作用力。结论阐明了灯盏乙素和牛血清白蛋白相互作用的机制,建立了灯盏乙素和牛血清白蛋白的结合模型。

关 键 词:中草药  灯盏乙素  牛血清白蛋白  荧光淬灭
修稿时间:2007-06-05

Study on the interaction between scutellarin and bovine serum albumin
WANG Li,ZHANG Ai-ping,YANG Jin-yan,YANG Bin-sheng. Study on the interaction between scutellarin and bovine serum albumin[J]. Chinese Remedies & Clinics, 2007, 7(9): 667-669
Authors:WANG Li  ZHANG Ai-ping  YANG Jin-yan  YANG Bin-sheng
Abstract:Objective To study the interaction between scutellarin and bovine serum albumin under virtual human physiology by fluorescence spectroscopy and ultraviolet spectroscopy. Methods According to scatchard′s model and Frster′s principle of non-radiation energy transferring, the binding parameters of scutellarin to bovine serum albumin were obtained by fluorescence quenching method. Results The binding parameters of scutellarin to bovine serum albumin were shown as: binding constant K=1.240×106, binding distance r=2.94 nm, with hydrophobic interaction between the two. Conclusion The binding mechanism and binding model were demonstrated by the binding parameters of scutellarin to bovine serum albumin.
Keywords:Drugs   Chinese Herbal  Scutellarin  Bovine serum albumin  Fluorescence quenching
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