scholarly journals Interactions of cyclodextrins and their derivatives with toxic organophosphorus compounds

2016 ◽  
Vol 12 ◽  
pp. 204-228 ◽  
Author(s):  
Sophie Letort ◽  
Sébastien Balieu ◽  
William Erb ◽  
Géraldine Gouhier ◽  
François Estour
Keyword(s):  
Organophosphorus Compound ◽  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Nerve Agents ◽  
Cyclic Structure ◽  
Biological Target

The aim of this review is to provide an update on the current use of cyclodextrins against organophosphorus compound intoxications. Organophosphorus pesticides and nerve agents play a determinant role in the inhibition of cholinesterases. The cyclic structure of cyclodextrins and their toroidal shape are perfectly suitable to design new chemical scavengers able to trap and hydrolyze the organophosphorus compounds before they reach their biological target.

scholarly journals Catalytic Degradation of Nerve Agents

Catalysts ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 881
Author(s):  
Agatino Zammataro ◽  
Rossella Santonocito ◽  
Andrea Pappalardo ◽  
Giuseppe Trusso Sfrazzetto
Keyword(s):  
World War Ii ◽  
Acute Toxicity ◽  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Lethal Effect ◽  
Nerve Agents ◽  
Catalytic Degradation ◽  
World War ◽  
Degradation Reactions ◽  
Chemical Hydrolysis

Nerve agents (NAs) are a group of highly toxic organophosphorus compounds developed before World War II. They are related to organophosphorus pesticides, although they have much higher human acute toxicity than commonly used pesticides. After the detection of the presence of NAs, the critical step is the fast decontamination of the environment in order to avoid the lethal effect of these organophosphorus compounds on exposed humans. This review collects the catalytic degradation reactions of NAs, in particular focusing our attention on chemical hydrolysis. These reactions are catalyzed by different catalyst categories (metal-based, polymeric, heterogeneous, enzymatic and MOFs), all of them described in this review.

scholarly journals Enzymatic Degradation of Organophosphorus Pesticides and Nerve Agents by EC: 3.1.8.2

Catalysts ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 1365
Author(s):  
Marek Matula ◽  
Tomas Kucera ◽  
Ondrej Soukup ◽  
Jaroslav Pejchal
Keyword(s):  
Catalytic Activity ◽  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Chemical Warfare Agents ◽  
Enzyme Commission Number ◽  
Nerve Agents ◽  
Organophosphorus Acid Anhydrolase ◽  
Warfare Agents ◽  
Heavy Burden ◽  
Medical Countermeasures

The organophosphorus substances, including pesticides and nerve agents (NAs), represent highly toxic compounds. Standard decontamination procedures place a heavy burden on the environment. Given their continued utilization or existence, considerable efforts are being made to develop environmentally friendly methods of decontamination and medical countermeasures against their intoxication. Enzymes can offer both environmental and medical applications. One of the most promising enzymes cleaving organophosphorus compounds is the enzyme with enzyme commission number (EC): 3.1.8.2, called diisopropyl fluorophosphatase (DFPase) or organophosphorus acid anhydrolase from Loligo Vulgaris or Alteromonas sp. JD6.5, respectively. Structure, mechanisms of action and substrate profiles are described for both enzymes. Wild-type (WT) enzymes have a catalytic activity against organophosphorus compounds, including G-type nerve agents. Their stereochemical preference aims their activity towards less toxic enantiomers of the chiral phosphorus center found in most chemical warfare agents. Site-direct mutagenesis has systematically improved the active site of the enzyme. These efforts have resulted in the improvement of catalytic activity and have led to the identification of variants that are more effective at detoxifying both G-type and V-type nerve agents. Some of these variants have become part of commercially available decontamination mixtures.

scholarly journals Assessment of four organophosphorus pesticides as inhibitors of human acetylcholinesterase and butyrylcholinesterase

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tena Čadež ◽  
Dora Kolić ◽  
Goran Šinko ◽  
Zrinka Kovarik
Keyword(s):  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Nerve Agents ◽  
Acute Poisoning ◽  
Health Concern ◽  
Common Mechanism ◽  
Standard Medical Therapy ◽  
Further Development ◽  
Kinetics Of

AbstractToxicity of organophosphorus compounds (OPs) remains a major public health concern due to their widespread use as pesticides and the existence of nerve agents. Their common mechanism of action involves inhibition of enzymes acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) which are crucial for neurotransmission. Both chronic and acute poisoning by OPs can leave long-lasting health effects even when the patients are treated with standard medical therapy. Therefore, an increasing urgency exists to find more effective oxime reactivators for compounds which are resistant to reactivation, especially phosphoramidates. Here, we investigated in silico and in vitro interactions and kinetics of inhibition for human cholinesterases with four organophosphate pesticides—ethoprophos, fenamiphos, methamidophos and phosalone. Overall, ethoprophos and fenamiphos displayed higher potency as inhibitors for tested cholinesterases. Our results show that methamidophos-inhibited hAChE was more susceptible to reactivation than hAChE inhibited by fenamiphos by selected oximes. Molecular modelling enabled an evaluation of interactions important for specificity and selectivity of both inhibition and reactivation of cholinesterases. Two newly developed reactivators—bispyridinium triazole oxime 14A and zwitterionic oxime RS194B possess remarkable potential for further development of antidotes directed against pesticides and related phosphoramidate exposures, such as nerve agents tabun or Novichoks.

scholarly journals Simultaneous Hydrolysis and Detection of Organophosphate by Benzimidazole Containing Ligand-Based Zinc(II) Complexes

Crystals ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 714
Author(s):  
Gaber A. M. Mersal ◽  
Hamdy S. El-Sheshtawy ◽  
Mohammed A. Amin ◽  
Nasser Y. Mostafa ◽  
Amine Mezni ◽  
...  
Keyword(s):  
Square Wave Voltammetry ◽  
Limit Of Detection ◽  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Carbon Paste ◽  
Square Wave ◽  
Wave Voltammetry ◽  
Carbon Past Electrode ◽  
Hydrolysis Of ◽  
Biomimetic Sensor

The agricultural use of organophosphorus pesticides is a widespread practice with significant advantages in crop health and product yield. An undesirable consequence is the contamination of soil and groundwater by these neurotoxins resulting from over application and run-off. Here, we design and synthesize the mononuclear zinc(II) complexes, namely, [Zn(AMB)2Cl](ClO4) 1 and [Zn(AMB)2(OH)](ClO4) 2 (AMB = 2-aminomethylbenzimidazole), as artificial catalysts inspired by phosphotriesterase (PTE) for the hydrolysis of organophosphorus compounds (OPs) and simultaneously detect the organophosphate pesticides such as fenitrothion and parathion. Spectral and DFT (B3LYP/Lanl2DZ) calculations revealed that complexes 1 and 2 have a square-pyramidal environment around zinc(II) centers with coordination chromophores of ZnN4Cl and ZnN4O, respectively. Both 1 and 2 were used as a modifier in the construction of a biomimetic sensor for the determination of toxic OPs, fenitrothion and parathion, in phosphate buffer by square wave voltammetry. The hydrolysis of OPs using 1 or 2 generates p-nitrophenol, which is subsequently oxidized at the surface of the modified carbon past electrode. The catalytic activity of 2 was higher than 1, which is attributed to the higher electronegativity of the former. The oxidation peak potentials of p-nitrophenol were obtained at +0.97 V (vs. Ag/AgCl) using cyclic voltammetry (CV) and +0.88 V (vs. Ag/AgCl) using square wave voltammetry. Several parameters were investigated to evaluate the performance of the biomimetic sensor obtained after the incorporation of zinc(II) complex 1 and 2 on a carbon paste electrode (CPE). The calibration curve showed a linear response ranging between 1.0 μM (0.29 ppm) and 5.5 μM (1.6 ppm) for fenitrothion and 1.0 μM (0.28 ppm) and 0.1 μM (0.028 ppm) for parathion with a limit of detection (LOD) of 0.08 μM (0.022 ppm) and 0.51 μM (0.149 ppm) for fenitrothion and parathion, respectively. The obtained results clearly demonstrated that the CPE modified by 1 and 2 has a remarkable electrocatalytic activity towards the hydrolysis of OPs under optimal conditions.

Developing acetylcholinesterase-based inhibition assay by modulated synthesis of silver nanoparticles: applications for sensing of organophosphorus pesticides

RSC Advances ◽  
2015 ◽  
Vol 5 (76) ◽  
pp. 61998-62006 ◽  
Author(s):  
D. Nanda Kumar ◽  
A. Rajeshwari ◽  
S. A. Alex ◽  
M. Sahu ◽  
A. M. Raichur ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Organophosphorus Compounds ◽  
Organophosphorus Pesticides ◽  
Inhibition Assay ◽  
Highly Sensitive

A novel and highly sensitive probe for the detection of organophosphorus compounds (OPs) using acetylcholinesterase (AChE) and acetylthiocholine (ATCh) during the modulated synthesis of silver nanoparticles.

scholarly journals Comparative determination of the efficacy of bispyridinium oximes in paraoxon poisoning / Usporedno određivanje učinkovitosti bispiridinijevih oksima pri trovanju paraoksonom

2015 ◽  
Vol 66 (2) ◽  
pp. 129-134 ◽  
Author(s):  
Suzana Žunec ◽  
Božica Radić ◽  
Kamil Kuča ◽  
Kamil Musilek ◽  
Ana Lucić Vrdoljak
Keyword(s):  
Therapeutic Efficacy ◽  
Standard Therapy ◽  
Organophosphorus Compounds ◽  
Nerve Agents ◽  
Therapeutic Efficiency ◽  
Hi 6 ◽  
Comparative Determination

Abstract The inability of standard therapy to provide adequate protection against poisoning by organophosphorus compounds (pesticides and nerve agents) motivated us to search for new, more effective oximes. We investigated the pharmacotoxicological properties of six experimental K-oximes (K027, K033, K048, K074, K075, and K203) in vivo. The therapeutic efficacy of K-oximes (at doses of 5 or 25 % of their LD50) combined with atropine was assessed in paraoxon-poisoned mice and compared with conventionally used oximes HI-6 and TMB-4. The bisoxime K074 was the most toxic (LD50=21.4 mg kg-1) to mice, while monoxime K027 was the least toxic (LD50=672.8 mg kg-1). With the exception of K033, all of the tested K-oximes showed better therapeutic efficiency than HI-6 and TMB-4. K027 and K048 stood out by demonstrating low acute toxicities and ensuring protective indices ranging from 60.0 to 100.0 LD50 of paraoxon. Taking into account that these two oximes showed a similar therapeutic efficacy regardless of the applied doses, our results suggest that K027 and K048 could be antidotes for paraoxon intoxication.

Inhibition of Aflatoxin Biosynthesis by Organophosphorus Compounds

1980 ◽  
Vol 43 (5) ◽  
pp. 381-384 ◽  
Author(s):  
M. F. DUTTON ◽  
M. S. ANDERSON
Keyword(s):  
Aspergillus Flavus ◽  
Organophosphorus Compound ◽  
Organophosphorus Compounds ◽  
Culture Fluid ◽  
Aflatoxin Production ◽  
The Other ◽  
Aflatoxin Biosynthesis ◽  
Inhibition Effect ◽  
Type Activity ◽  
Acetate Derivative

The effect of a range of organophosphorus and various other compounds on production of aflatoxin by Aspergillus flavus was investigated. Five organophosphorus compounds - Chlormephos, Ciodrin, Naled, Phosdrin and Trichlorphon- at concentrations of 20 and 100 μg/ml of culture fluid were found to have activity similar to Dichlorvos, in that they lowered the level of aflatoxin produced and caused formation of several anthraquinone pigments. Two of these pigments have not previously been described, one was named Versicol and a suggested structure is presented, whilst the other compound was shown to be its acetate derivative. A rationale is suggested for the required elements of structure, which are necessary for an organophosphorus compound to have Dichlorvos-type activity. Two unrelated compounds, ammonium nitrate and Tridecanone were also found to elicit Dichlorvos-type activity. It is likely that tridecanone or its breakdown products competitively inhibit enzymes involved in aflatoxin biosynthesis. It is possible that this inhibition effect explains the lowering of aflatoxin production in lipid-rich commodities infected by A. flavus.

scholarly journals Characterization of [3H]di-isopropyl phosphorofluoridate-binding proteins in hen brain. Rates of phosphorylation and sensitivity to neurotoxic and non-neurotoxic organophosphorus compounds

1985 ◽  
Vol 228 (3) ◽  
pp. 537-544 ◽  
Author(s):  
C D Carrington ◽  
M B Abou-Donia
Keyword(s):  
Organophosphorus Compound ◽  
Binding Proteins ◽  
Organophosphorus Compounds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reaction Rates ◽  
Binding Activity ◽  
Binding Characteristics ◽  
Delayed Neurotoxicity ◽  
Neurotoxic Esterase

The experiments described in this paper were designed to isolate [3H]di-isopropyl phosphorofluoridate-binding proteins by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis for the purpose of characterizing and identifying potential initiation sites for organophosphorus-compound-induced delayed neurotoxicity. The major Paraoxon-insensitive Mipafox-sensitive binding protein (Mr 160 000) was found to be identical with one previously identified as neurotoxic esterase, an enzyme that has been proposed to be the target site for organophosphorus-compound-induced delayed neurotoxicity. However, two other binding proteins with suitable binding characteristics were also found in smaller amounts, one of which has not been detected previously. Di-isopropyl phosphorofluoridate was found to phosphorylate all three of these proteins at rates similar to the rate at which neurotoxic esterase is inhibited by di-isopropyl phosphorofluoridate. Varying the concentration of di-isopropyl phosphorofluoridate or the time of incubation produced similar increases in binding to each of the labelled proteins. This suggests that the reaction rates of di-isopropyl phosphorofluoridate with proteins may be described by first-order kinetics, and the concentration of the Michael is complex formed during binding is minimal for all the phosphorylated proteins. The recovery of the binding activity in the 160 000-Mr band was found to be similar to the recovery of neurotoxic esterase activity, lending further support to the contention that this band is identical with neurotoxic esterase.

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