期刊
JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS
卷 55, 期 2, 页码 265-271出版社
ELSEVIER
DOI: 10.1016/j.jpba.2011.01.033
关键词
Ligand; Plasmodium falciparum; Thioredoxin reductase; Liquid chromatography/mass spectrometry; Ultrafiltration
资金
- American Society of Pharmacognosy
In our study, we have screened 133 structurally diverse natural compounds from the MEGx (R) collection of AnalytiCon Discovery and three synthetic hispolone analogs for binding affinity to Plasmodium falciparum thioredoxin reductase (pfTrxR) using an ultrafiltration (UF) and liquid chromatography (LC/MS) based ligand-binding assay newly developed in our laboratory. PfTrxR catalyzes the reduction of thioredoxin (PfTrx) protein. In reduced form, PfTrx is essentially involved in the antioxidative defense and redox regulation of P. falciparum. Nine compounds (yohimbine (1), catharanthine (2), vobasine (3), gnetifolin E (4), quinidine N-oxide (5), 11-hydroxycoronaridine (6), hispolone (7), hispolone methyl ether (8), and hernagine (9)) displayed binding affinity for pfTrxR at 1 mu M. The ranking order of compound's binding affinities for PfTrxR is 7 > 6 > 2 > 4 > 5 > 8 > 1 > 9 > 3. On the other hand, compounds 6, 7, 2 and 8 demonstrated specific binding to the active site of PfTrxR, when ligands were tested in an equimolar mixture of 1 mu M. (C) 2011 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据