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Monoamine oxidase B immobilized on magnetic nanoparticles for screening of the enzyme's inhibitors from herbal extracts

机译:在磁性纳米粒子上固定的单胺氧化酶B用于从草药提取物中筛选酶的抑制剂

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Monoamine oxidase B (MAO-B) was for the first time immobilized on magnetic nanoparticles to be used for screening of MAO-B inhibitors from herbal extracts. The immobilized enzyme was characterized with transmission electronic microscopy, Fourier transform infrared spectroscopy, thermal gravimetric analysis, and vibrating sample magnetometer. The immobilized enzyme retained 95% of the activity, while the thermostability was significantly increased. It was then used as solid phase extraction absorbent to extract MAO-B's ligands from two traditional Chinese medicinal plants, Cortex fraxini and Pericarpium granati. Calceolarioside B and ellagic acid were extracted from C. fraxini and P. granati, respectively, and both of them were found to be inhibitors of MAO-B with IC50 of 40.95 +/- 0.63 and 103.70 +/- 2.34 mu M, respectively. This is the first report that calceolarioside B inhibits MAO-B activity. Furthermore, inhibitory mechanisms of both compounds were studied by molecular docking analysis, the results of which demonstrated that the affinity of calceolarioside B with monoamine oxidase B was stronger than that of ellagic acid. The method proposed in this work is highly efficient for screening of MAO-B inhibitors from complex mixtures, showing great potential in discovering anti-Parkinson's disease compounds present in medicinal plants.
机译:单胺氧化酶B(MAO-B)首次固定在磁性纳米颗粒上以用于筛选来自草药提取物的MAO-B抑制剂。固定化酶的特征在于透射电子显微镜,傅里叶变换红外光谱,热重分析和振动样品仪。固定化酶保留了95%的活性,而热稳定性显着增加。然后用作固相萃取吸收剂,从两个中药植物,皮质Fraxini和Pericarpium granati中提取Mao-B的配体。分别从C.Fraxini和P.Granati中提取Calceolarioside B和鞣花酸,并发现它们两者都是MAO-B的抑制剂,IC50分别为40.95 +/- 0.63和103.70 +/- 2.34 mu m。这是Calceolarioside B抑制MAO-B活动的第一份报告。此外,通过分子对接分析研究了两种化合物的抑制机制,结果表明Calceolarioside B与单胺氧化酶B的亲和力比鞣花酸的亲和力强。本作作品中提出的方法高效筛选来自复杂混合物的MAO-B抑制剂,显示出发现药用植物中存在的抗帕金森病化合物的巨大潜力。

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