728865-23-4

Basic information

• Product Name: CHIR-090
• Synonyms: CHIR-090;N-[(1S,2R)-2-Hydroxy-1-[(hydroxyamino)carbonyl]propyl]-4-[[4-(4-morpholinylmethyl)phenyl]ethynyl]benzamide
• CAS NO: 728865-23-4
• Molecular Formula: C₂₄H₂₇N₃O₅
• Molecular Weight: 437.48828
• Mol File: 728865-23-4.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• Density: 1.33±0.1 g/cm3(Predicted)
• Solubility: ≥21.85 mg/mL in DMSO; insoluble in EtOH; insoluble in H2O
• PKA: 9.11±0.40(Predicted)
• CAS DataBase Reference: CHIR-090(CAS DataBase Reference)
• NIST Chemistry Reference: CHIR-090(728865-23-4)
• EPA Substance Registry System: CHIR-090(728865-23-4)

Safety Data

• Hazardous Substances Data: 728865-23-4(Hazardous Substances Data)

Usage

Description

CHIR-090 is the first reported compound that in fact kills both E. coli and Pseudomonas aeruginosa in bacterial disk diffusion assays (Liang et al. 2011). Nonetheless, CHIR-090 was about 600-fold less effective against LpxC orthologs from the Rhizobiaceae family than against E. coli LpxC. In this way, studies have shown that the removal of morpholine ring, based on a chemical scaffold of reduced radius, was able to increase affinity by 20-fold for LpxC enzymes from the Rhizobiaceae family of bacteria and enhance the antibiotic activity against E. coli and P. aeruginosa by 2–4 fold over CHIR-090.

Upstream product

• 110-91-8 morpholine 
• 728878-11-3 (2S,3R)-2-[4-(4-formylphenylethynyl)benzoylamino]-3-hydroxybutyric acid methyl ester 
• 15164-44-0 p-(iodophenyl)carboxaldehyde 
• 728878-12-4 (2S,3R)-3-hydroxy-2-[4-(4-morpholin-4-ylmethylphenylethynyl)benzoylamino]butyric acid methyl ester 
• 728878-24-8 (2S,3R)-2-(4-ethynylbenzoylamino)-3-hydroxybutanoic acid methyl ester 
• 144693-65-2 4-ethynylbenzoic acid sodium salt 
• 75867-41-3 4-trimethylsilanylethynyl-benzoic acid methyl ester 
• 619-44-3 methyl 4-iodobenzoate 

Relevant articles and documents

COMPOUNDS FOR THE TREATMENT OF BOVINE OR SWINE RESPIRATORY DISEASE

The present invention provides compounds for use in the treatment of respiratory diseases of animals, especially Bovine or Swine Respiratory disease (BRD and SRD).

Exploring the UDP pocket of LpxC through amino acid analogs

Lipopolysaccharide (LPS) biosynthesis is an attractive antibacterial target as it is both conserved and essential for the survival of key pathogenic bacteria. Lipid A is the hydrophobic anchor for LPS and a key structural component of the outer membrane of Gram-negative bacteria. Lipid A biosynthesis is performed in part by a unique zinc dependent metalloamidase, LpxC (UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase), which catalyzes the first non-reversible step in lipid A biosynthesis. The UDP portion of the LpxC substrate-binding pocket has been relatively unexplored. We have designed and evaluated a series of hydroxamate based inhibitors which explore the SAR of substitutions directed into the UDP pocket with a range of substituted α-amino acid based linkers. We also provide the first wild type structure of Pseudomonas aeruginosa LpxC which was utilized in the design of many of these analogs.