820-11-1Relevant articles and documents
Oxidase-mimicking activity of ultrathin MnO2 nanosheets in a colorimetric assay of chlorothalonil in food samples
Dai, Zhihui,Li, Zhenxi,Lu, Yuxiao,Sheng, Enze,Tan, Yuting,Xiao, Yue
, (2020/07/02)
Chlorothalonil is a class of 2B carcinogen which is widely used in the prevention and treatment of fungal diseases in food samples. Its residual problem has been increasingly concerned by society. In this paper, a fast and simple colorimetric assay based on Manganese dioxide nanosheets (MnO2 NSs)-oxidize 3,3′,5,5′-tetramethylbenzidine (TMB) platform was used to detect residual pesticide chlorothalonil in food samples. Under optimal conditions, the half maximal inhibitory concentration and the limit of detection of chlorothalonil were 3.27 and 0.024 ng/mL. There were no obvious cross-reactivity between chlorothalonil and interference substances. The recoveries shown the satisfactory results. The results of colorimetric assay for the authentic samples were largely consistent with gas chromatography. Therefore, the proposed method would be convenient and satisfactory analytical methods for the monitoring of chlorothalonil. Furthermore, the MnO2 – TMB system was used to produce test strips for quick and convenient visual detection of chlorothalonil with good performance.
Broad specificity of human phosphoglycerate kinase for antiviral nucleoside analogs
Gallois-Montbrun, Sarah,Faraj, Abdesslem,Seclaman, Edward,Sommadossi, Jean-Pierre,Deville-Bonne, Dominique,Véron, Michel
, p. 1749 - 1756 (2007/10/03)
Nucleoside analogs used in antiviral therapies need to be phosphorylated to their tri-phospho counterparts in order to be active on their cellular target. Human phosphoglycerate kinase (hPGK) was recently reported to participate in the last step of phosphorylation of cytidine l-nucleotide derivatives [Krishnan PGE, Lam W, Dutschman GE, Grill SP, Cheng YC. Novel role of 3-phosphoglycerate kinase, a glycolytic enzyme, in the activation of l-nucleoside analogs, a new class of anticancer and antiviral agents. J Biol Chem 2003;278:36726-32]. In the present work, we extended the enzymatic study of human PGK specificity to purine and pyrimidine nucleotide derivatives in both d- and l-configuration. Human PGK demonstrated catalytic efficiencies in the 104-10 5 M-1 s-1 range for purine ribo-, deoxyribo- and dideoxyribonucleotide derivatives, either in d- or l-configuration. In contrast, it was poorly active with natural pyrimidine d-nucleotides (less than 103 M-1 s-1). Pyrimidine l-enantiomers, which are promising therapeutic analogs against B hepatitis, were 2-25 times better substrates than their d-counterparts. The broad specificity of substrate of human PGK suggests that this enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, l-2′-deoxycytosine and l-2′-deoxythymidine.
The synthesis of novel bisphosphonates as inhibitors of phosphoglycerate kinase (3-PGK)
Caplan, Neil A.,Pogson, Christopher I.,Hayes, David J.,Blackburn, G. Michael
, p. 421 - 437 (2007/10/03)
A series of conformationally-restrained analogues of 1,3-bisphospho-D-glyceric acid (1,3-BPG) 1 has been synthesised for use as inhibitors of 3-PGK (E.C. 2.7.2.3). These compounds have non-scissile phosphonate linkages and also incorporate α-halogen substituents to make them isopolar and isosteric mimics of the natural substrate. A monocyclic aryl core between the two phosphoryl centres provides both a rigid framework linking these moieties and loci for further substitution. The compounds were tested against human 3-PGK and found to be good competitive inhibitors. α-Fluorination of the phosphonic acids increased the affinity for the enzyme into the submicromolar range. Correlation of IC50 data with pKa. and pKa, values indicates that the acidity of the phosphoryl group exerts a strong influence on protein binding. The Royal Society of Chemistry 2000.
