4088-26-0

Basic information

• Product Name: Nonanoic acid, 9-amino-, methyl ester
• CAS NO: 4088-26-0
• Molecular Formula: C10H21NO2
• Molecular Weight: 187.282
• Mol File: 4088-26-0.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: Nonanoic acid, 9-amino-, methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Nonanoic acid, 9-amino-, methyl ester(4088-26-0)
• EPA Substance Registry System: Nonanoic acid, 9-amino-, methyl ester(4088-26-0)

Safety Data

• Hazardous Substances Data: 4088-26-0(Hazardous Substances Data)

Upstream product

• 112-62-9 octadec-9-enoic acid methyl ester 
• 13481-97-5 dimethyl (Z)-octadec-9-ene-1,18-dioate 
• 167493-50-7 9-Isocyanato-nonanoic acid methyl ester 
• 186581-53-3 diazomethane 
• 181486-90-8 N,N'-diacetyl(10,11-⁽²⁾H₂)-inandenin-12-one 
• 83633-04-9 N-[4-(9,18-Dioxo-octadecahydro-4a,8-diaza-benzocycloheptadecen-8-yl)-butyl]-acetamide 

Downstream Products

• 154-92-7 Nα-benzoyl-L-arginine 
• 1120-12-3 9-aminononanoic acid 

Relevant articles and documents

SYNTHESIS OF OMEGA-AMINO CARBOXYLIC ACIDS AND THEIR ESTERS FROM UNSATURATED FATTY ACID DERIVATIVES

The invention relates to a process for preparing omega-amino acids or their esters, which is characterized by the following steps: c) ozonolysis of unsaturated fatty acids or fatty acid derivatives,d) reductive amination of the reaction mixture obtained from the reaction with ozone, to give the omega-amino acid or ester thereof, the reaction being carried out with a C1-C5 alcohol in a mixture with at least 0.5% by weight of water as solvent, based on the total amount of solvent.

Design, synthesis, and biochemical evaluation of N-substituted maleimides as inhibitors of prostaglandin endoperoxide synthases

N-(Carboxyalkyl)maleimides are rapid as well as time-dependent inhibitors of prostaglandin endoperoxide synthase (PGHS). The corresponding N- alkylmaleimides were only time-dependent inactivators of PGHS, suggesting that the carboxylate is critical for rapid inhibition. Several N-substituted maleimide analogs containing structural features similar to those of the nonsteroidal anti-inflammatory drug aspirin were synthesized and evaluated as inhibitors of PGHS. Most of the aspirin-like maleimides inactivated the cyclooxygenase activity of purified ovine PGHS-1 in a time- and concentration-dependent manner similar to that of aspirin. The peroxidase activity of PGHS was also inactivated by the maleimide analogs. The cyclooxygenase activity of the inducible isozyme, i.e., PGHS-2, was also inhibited by these compounds. The corresponding succinimide analog of N-5- maleimido-2-acetoxy-1-benzoic acid did not inhibit either enzyme activity, suggesting that inactivation was due to covalent modification of the protein. The mechanism of inhibition of PGHS-1 by N-(carboxyheptyl)maleimide was investigated. Incubation of apoPGHS-1 with 2 equiv of N-(carboxyheptyl)[3,4- 14C]maleimide led to the incorporation of radioactivity in the protein, but no adduct was detected by reversed-phase HPLC, suggesting that it was unstable to the chromatographic conditions. Furthermore, hematin- reconstituted PGHS-1, which was rapidly inhibited by N- (carboxyheptyl)maleimide, displayed spontaneous regeneration of about 50% of the cyclooxygenase and peroxidase activities, suggesting that the adduct responsible for the inhibition breaks down to regenerate active enzyme. ApoPGHS-1, inhibited by N-(carboxyheptyl)maleimide, did not display regeneration of enzyme activity, but addition of hematin to the inhibited apoenzyme led to spontaneous recovery of about 50% of cyclooxygenase activity. These results suggest that addition of heme leads to a conformational change in the protein which increases the susceptibility of the adduct toward hydrolytic cleavage. ApoPGHS-1, pretreated with N(carboxyheptyl)maleimide, was resistant to trypsin cleavage, suggesting that the carboxylate functionality of the maleimide binds in the cyclooxygenase channel. A model for the interaction of N-(carboxyheptyl)maleimide in the cyclooxygenase active site is proposed.