Potential antifungal activity and structure-activity relationships of some 2-amino acid substituted benzo-1,3,2-dioxaphospholene, oxazaphospholine and diazaphospholine 2-ones

Ali, Hussein M.; Ali, M. K.

doi:10.1007/s001280000024

Cited by 3 publications

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These compounds inhibited, in vitro, 29-76% of rat serum AChE activity at level of 1 ppm. In addition, they showed good insecticidal and potential fungicidal activities compared with various commercial pesticides [14,15]. The present article examines the effects of these phosphoramidates, in vivo, on the inhibition and recovery of serum, liver and brain AChE in comparison with a moderate toxic commercial pesticide, fenitrothion [16,17].…”

Section: Introductionmentioning

confidence: 99%

Inhibition and recovery of serum, liver and brain acetylcholinesterase activities in rats exposed to new groups ofO-ethyl phosphoramidates and benzo-1,3,2-dioxaphospholenes

Ali¹,

Attia²,

Eldeen³

2004

Toxicological & Environmental Chemistry

View full text Add to dashboard Cite

Searching for new organophosphorus compounds with minimum effects on acetylcholinesterase of non-target organism especially mammals has gained an increased attention in the public concern. In this effort, the effects of some recently introduced O-ethyl phosphoramidates and benzo-1,3,2-dioxaphospholenes on rat acetylcholinesterase in different tissues have been evaluated in vivo and compared with the effects of fenitrothion, a commercial pesticide with reported moderate toxicity to mammals. The tested compounds were introduced orally in a single dose of 85 mg/kg body weight. Results indicated that the tested phosphoramidates lowered the enzyme activity to 54-69, 36-71 and 70-76% of its normal activity in serum, liver and brain, respectively. Meanwhile, the enzyme activity was depressed by fenitrothion to 11, 2 and 11% in the mentioned organs respectively. The lower anticholinesterase activity of the examined phosphoramidates than that of fenitrothion was attributed to their low hydrophobicity and low electrophilicity of their phosphorus atom, which reduces their interaction with the enzyme active site.

show abstract

Section: Introductionmentioning

confidence: 99%