Synthesis, Biological Evaluation and In Silico Computational Studies of 7-Chloro-4-(1-1,2,3-triazol-1-yl)quinoline Derivatives: Search for New Controlling Agents against (Lepidoptera: Noctuidae) Larvae.

Clicks: 345
ID: 4774
2019
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Emerging

Ranked #58 of 850 articles by views in Journal of agricultural and food chemistry

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 850 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
The insecticidal and antifeedant activities of five 7-chloro-4-(1-1,2,3-triazol-1-yl)quinoline derivatives were evaluated against the maize armyworm, (J.E. Smith). These hybrids were prepared through a copper-catalyzed azide alkyne cycloaddition (CuAAC, known as a click reaction) and displayed larvicidal properties with LD values below 3 mg/g insect, and triazolyl-quinoline hybrid showed an LD of 0.65 mg/g insect, making it 2-fold less potent than methomyl, which was used as a reference insecticide (LD = 0.34 mg/g insect). Compound was the most active antifeedant derivative (CE = 162.1 μg/mL) with a good antifeedant index (56-79%) at concentrations of 250-1000 μg/mL. Additionally, triazolyl-quinoline hybrids - exhibited weak inhibitory activity against commercial acetylcholinesterase from (electric-eel AChE) (IC = 27.7 μg/mL) as well as low anti-ChE activity on larvae homogenate (IC = 68.4 μg/mL). Finally, molecular docking simulations suggested that hybrid binds to the catalytic active site (CAS) of this enzyme and around the rim of the enzyme cavity, acting as a mixed (competitive and noncompetitive) inhibitor like methomyl. Triazolyl-quinolines - and inhibit AChE by binding over the perimeter of the enzyme cavity, functioning as noncompetitive inhibitors. The results described in this work can help to identify lead triazole structures from click chemistry for the development of insecticide and deterrent products against and related insect pests.
Reference Key
rosadosolano2019synthesisjournal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors
Journal Journal of agricultural and food chemistry
Year 2019
DOI
10.1021/acs.jafc.9b01067
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.