1798-03-4

Usage

Uses

Used in Agricultural and Horticultural Applications:
(2-Ethyl-phenoxy)-acetic acid is used as a herbicide for controlling weeds and promoting the growth of desirable plants. Its ability to disrupt the synthesis of plant hormones makes it an effective tool in managing vegetation and ensuring the health and productivity of crops.
Used in Research and Development:
In addition to its practical applications, (2-Ethyl-phenoxy)-acetic acid is also utilized in the research and development of new herbicide compounds. Its unique properties and mechanism of action provide valuable insights for the creation of innovative and more effective herbicides to address the evolving needs of agriculture and horticulture.

InChI:InChI=1/C10H12O3/c1-2-8-5-3-4-6-9(8)13-7-10(11)12/h3-6H,2,7H2,1H3,(H,11,12)/p-1

Upstream product

• 90-00-6 o-Hydroxyethylbenzene 
• 79-11-8 chloroacetic acid 
• 100256-84-6 ethyl 2-(2-ethylphenoxy)acetate 
• 861143-60-4 (2-Ethyl-phenoxy)-acetic acid methyl ester 

Downstream Products

• 90-00-6 o-Hydroxyethylbenzene 
• 124-38-9 carbon dioxide 
• 201230-82-2 carbon monoxide 
• 100256-84-6 ethyl 2-(2-ethylphenoxy)acetate 

Relevant academic research and scientific papers

Design, synthesis and biological evaluation of oxime lacking Psammaplin inspired chemical libraries as anti-cancer agents

In this study, we attempted the chemical simplification of Psammaplin (PsA), while retaining its activity in vitro. Inspired by the previous Structure Activity Relationship (SAR) studies on various PsA analogues and relying on the fact that oxime is metabolically unstable, we initially designed and synthesized a diverse library of PsA analogues and evaluated for cytotoxic activity. Among 32 compounds of Psammaplin analogues synthesized, the compound 10b was almost equally active as parent Psammaplin in vitro.

Discovery of Novel UDP- N-Acetylglucosamine Acyltransferase (LpxA) Inhibitors with Activity against Pseudomonas aeruginosa

This study describes a novel series of UDP-N-acetylglucosamine acyltransferase (LpxA) inhibitors that was identified through affinity-mediated selection from a DNA-encoded compound library. The original hit was a selective inhibitor of Pseudomonas aeruginosa LpxA with no activity against Escherichia coli LpxA. The biochemical potency of the series was optimized through an X-ray crystallography-supported medicinal chemistry program, resulting in compounds with nanomolar activity against P. aeruginosa LpxA (best half-maximal inhibitory concentration (IC50) 20 μM and MIC > 128 μg/mL). The mode of action of analogues was confirmed through genetic analyses. As expected, compounds were active against multidrug-resistant isolates. Further optimization of pharmacokinetics is needed before efficacy studies in mouse infection models can be attempted. To our knowledge, this is the first reported LpxA inhibitor series with selective activity against P. aeruginosa.