17722-71-3

Usage

Uses

Used in Pharmaceutical Industry:
N-(3,4-DICHLORO-PHENYL)-SUCCINAMIC ACID is used as a building block for the synthesis of various drugs, contributing to the development of new compounds with therapeutic value.
Used in Agrochemical Industry:
N-(3,4-DICHLORO-PHENYL)-SUCCINAMIC ACID is used as a component in the creation of herbicides and pesticides, enhancing the effectiveness of these products in agricultural applications.
Additionally, due to its potential biological activity, N-(3,4-DICHLORO-PHENYL)-SUCCINAMIC ACID serves as a valuable tool for researchers and chemists in exploring and developing new compounds with either medicinal or agricultural significance.

InChI:InChI=1/C10H10Cl2N2O2/c11-7-2-1-6(5-8(7)12)14-10(16)4-3-9(13)15/h1-2,5H,3-4H2,(H2,13,15)(H,14,16)

Upstream product

• 108-30-5 succinic acid anhydride 
• 95-76-1 m,p-dichloroaniline 

Downstream Products

• 860425-55-4 N-(4,5-dichloro-2-nitro-phenyl)-succinamic acid 
• 23115-73-3 (C₄H₉)3SnOOCCH₂CH₂CONHC₆H₃Cl₂ 
• 857753-41-4 N-(2-amino-4,5-dichloro-phenyl)-succinamic acid 

Relevant academic research and scientific papers

Tackling Pseudomonas aeruginosa Virulence by a Hydroxamic Acid-Based LasB Inhibitor

In search of novel antibiotics to combat the challenging spread of resistant pathogens, bacterial proteases represent promising targets for pathoblocker development. A common motif for protease inhibitors is the hydroxamic acid function, yet this group has often been related to unspecific inhibition of various metalloproteases. In this work, the inhibition of LasB, a harmful zinc metalloprotease secreted by Pseudomonas aeruginosa, through a hydroxamate derivative is described. The present inhibitor was developed based on a recently reported, highly selective thiol scaffold. Using X-ray crystallography, the lack of inhibition of a range of human matrix metalloproteases could be attributed to a distinct binding mode sparing the S1′ pocket. The inhibitor was shown to restore the effect of the antimicrobial peptide LL-37, decrease the formation of P. aeruginosa biofilm and, for the first time for a LasB inhibitor, reduce the release of extracellular DNA. Hence, it is capable of disrupting several important bacterial resistance mechanisms. These results highlight the potential of protease inhibitors to fight bacterial infections and point out the possibility to achieve selective inhibition even with a strong zinc anchor.

Antibacterially Active Substituted Anilides of Carboxylic and Sulfonic Acids

Anilides of carboxylic and sulfonic acids were prepared and tested for antimicrobial activity.While these anilides were ineffective against Gram-negative organisms, there was good correlation between chemical structure and biological activity against Gram-positive species.Both the nature and position of the benzene ring substituents and the length of the carbon side chain affected the activity and specificity of the compounds.The highest activity was observed when the acyl or sulfuryl moiety had a C7-C9 side chain attached.The CONH and SO2NH bridging groups wereequally effective.The attachment of COOH or COOCH3 groups in the ω-position did not effect activity, but the substitution of the acidic proton of the sulfonamide group by an alkyl group rendered the compound inactive.Six compounds, which were substituted anilides of sulfonic acids, fatty acids, or the analogues α-methylene-substituted acids, were bacteriostatic at 10 ppm against Bacillus cereus, Staphylococcus aureus, Streptococcus faecalis and Lactobacillus plantarum .One of these compounds, 2-hydroxy-5-nitroanilide of α-methylenedecanoic acid, was bactericidal at 1 ppm.