Human erythrocyte and brain acetylcholinesterase are preferentially inhibited by the P(-)-isomers of C(+/-)P(+/-)-soman. The enzymes inhibited by the P(-)-isomers behave similarly with respect to oxime-induced reactivation and aging. HI-6 is the best reactivator for C(+)P(-)-soman-inhibited acetylcholinesterases. Oxime-induced reactivation of the C(-)P(-)-soman-inhibited acetylcholinesterases is much more difficult to achieve.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0167-4838(85)90294-8 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Stable hemiaminals from axially chiral pyridine compounds.
Chirality
June 2023
Department of Chemistry, Bogazici University, Istanbul, Turkey.
In this study, we have synthesized a series of 3-(pyridin-2-yl)-2-(pyridin-2-ylimino)thiazolidin-4-ol derivatives regioselectively from 2-iminothiazolidin-4-ones using LiAlH at room temperature. Due to the presence of the restricted rotation around the N3-C single bond, the formation of M/P isomers was observed. The OH group of the hemiaminal was found to orient itself on the same side with pyridyl nitrogen during this restricted rotation to form an intramolecular hydrogen bond, which was demonstrated by the computational DFT study.
View Article and Find Full Text PDFSynthesis and evaluation of the inhibitory activity of the four stereoisomers of the potent and selective human γ-glutamyl transpeptidase inhibitor GGsTop.
Bioorg Med Chem Lett
November 2017
Institute for Chemical Research, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
2-Amino-4-{[3-(carboxymethyl)phenoxy](methoxy)phosphoryl}butanoic acid (GGsTop) is a potent, highly selective, nontoxic, and irreversible inhibitor of γ-glutamyl transpeptidase (GGT). GGsTop has been widely used in academic and medicinal research, and also as an active ingredient (Nahlsgen) in commercial anti-aging cosmetics. GGsTop consists of four stereoisomers due to the presence of two stereogenic centers, i.
View Article and Find Full Text PDFPost-exposure treatment of VX poisoned guinea pigs with the engineered phosphotriesterase mutant C23: a proof-of-concept study.
Toxicol Lett
November 2014
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.
The highly toxic organophosphorus (OP) nerve agent VX is characterized by a remarkable biological persistence which limits the effectiveness of standard treatment with atropine and oximes. Existing OP hydrolyzing enzymes show low activity against VX and hydrolyze preferentially the less toxic P(+)-VX enantiomer. Recently, a phosphotriesterase (PTE) mutant, C23, was engineered towards the hydrolysis of the toxic P(-) isomers of VX and other V-type agents with relatively high in vitro catalytic efficiency (kcat/KM=5×10(6)M(-1)min(-1)).
View Article and Find Full Text PDFEvolved stereoselective hydrolases for broad-spectrum G-type nerve agent detoxification.
Chem Biol
April 2012
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
A preferred strategy for preventing nerve agents intoxication is catalytic scavenging by enzymes that hydrolyze them before they reach their targets. Using directed evolution, we simultaneously enhanced the activity of a previously described serum paraoxonase 1 (PON1) variant for hydrolysis of the toxic S(P) isomers of the most threatening G-type nerve agents. The evolved variants show ≤340-fold increased rates and catalytic efficiencies of 0.
View Article and Find Full Text PDFChromatographic preparation and kinetic analysis of interactions between tabun enantiomers and acetylcholinesterase.
Toxicol Lett
June 2010
Bundeswehr Institute of Pharmacology and Toxicology, Neuherbergstrasse 11, 80937 Munich, Germany.
The easy accessibility to highly toxic OP (organophosphorus)-type chemical warfare agents (nerve agents) underlines the necessity for an effective medical treatment. Acute OP toxicity is primarily caused by inhibition of acetylcholinesterase (AChE, EC 3.1.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!