4303-70-2

Usage

Uses

Used in Pharmaceutical Industry:
(E)-9-Octadecenamide is used as a sleep-inducing agent for its ability to promote physiological sleep in rats. Its sleep-inducing properties make it a potential candidate for the development of therapeutics aimed at treating sleep disorders and improving sleep quality.
Used in Enzyme Inhibition:
(E)-9-Octadecenamide is used as an inhibitor of rat microsomal epoxide hydrolase (mEH) and phospholipase A2 (PLA2) enzymes. Its inhibitory effects on these enzymes can be leveraged in the development of drugs targeting various diseases and conditions where these enzymes play a role.
Used in Research and Development:
(E)-9-Octadecenamide serves as a valuable compound for research purposes, particularly in the study of sleep mechanisms, enzyme inhibition, and the development of novel therapeutics. Its unique properties and interactions with biological systems make it an important tool for scientific investigations in various fields, including neuroscience, pharmacology, and biochemistry.

InChI:InChI=1/C18H35NO/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(19)20/h9-10H,2-8,11-17H2,1H3,(H2,19,20)/b10-9+

Upstream product

• 537-39-3 trielaidin 
• 112-77-6 (Z)-9-octadecenoyl chloride 
• 112-79-8 Elaidic acid 
• 77287-34-4 formamide 
• 112-77-6 elaidoyl chloride 
• 55726-25-5 elaidic acid-anhydride 
• 79-37-8 oxalyl dichloride 

Downstream Products

• 112-90-3 oleylamine 
• 112-90-3 trans-oleylamine 
• 116749-36-1 trans-8-heptadecenylammonium tosylate 

Relevant academic research and scientific papers

Electrospray ionization and collision induced dissociation mass spectrometry of primary fatty acid amides

Primary fatty acid amides are a group of bioactive lipids that have been linked with a variety of biological processes such as sleep regulation and modulation of monoaminergic systems. As novel forms of these molecules continue to be discovered, more emphasis will be placed on selective, trace detection. Currently, there is no published experimental determination of collision induced dissociation of PFAMs. A select group of PFAM standards, 12 to 22 length carbon chains, were directly infused into an electrospray ionization source Quadrupole Time of Flight Mass Spectrometer. All standards were monitored in positive mode using the [M + H]+ peak. Mass Hunter Qualitative Analysis software was used to calculate empirical formulas of the product ions. All PFAMs showed losses of 14 m/z indicative of an acyl chain, while the monounsaturated group displayed neutral losses corresponding to H2O and NH3. The resulting spectra were used to propose fragmentation mechanisms. Isotopically labeled PFAMs were used to validate the proposed mechanisms. Patterns of saturated versus unsaturated standards were distinctive, allowing for simple differentiation. This determination will allow for fast, qualitative identification of PFAMs. Additionally, it will provide a method development tool for selection of unique product ions when analyzed in multiple reaction monitoring mode.

Process for the preparation of saturated or unsaturated primary fatty amines

Process for the preparation of unsaturated and saturated primary fatty amines comprising the steps of chlorination, treatment by ammonia, reduction and purification

Fatty-acid amide hydrolase

The soporific activity of cis-9,10-octadecenoamide and other soporific fatty acid primary amides is neutralized by hydrolysis in the presence of fatty-acid amide hydrolase (FAAH). Hydrolysis of cis-9,10-octadecenoamide by FAAH leads to the formation of oleic acid, a compound without soporific activity. FAAH has be isolated and the gene encoding FAAH has been cloned, sequenced, and used to express recombinant FAAH. Inhibitors of FAAH are disclosed to block the hydrolase activity.

Inhibition of microsomal epoxide hydrolases by ureas, amides, and amines

The microsomal epoxide hydrolase (mEH) plays a significant role in the metabolism of xenobiotics such as polyaromatic toxicants. Additionally, polymorphism studies have underlined a potential role of this enzyme in relation to several diseases, such as emphysema, spontaneous abortion, and several forms of cancer. To provide new tools for studying the function of mEH, inhibition of this enzyme was investigated. Inhibition of recombinant rat and human mEH was achieved using primary ureas, amides, and amines. Several of these compounds are more potent than previously published inhibitors. Elaidamide, the most potent inhibitor that is obtained, has a Ki of 70 nM for recombinant rat mEH. This compound interacts with the enzyme forming a noncovalent complex, and blocks substrate turnover through an apparent mix of competitive and noncompetitive inhibition kinetics. Furthermore, in insect cell cultures expressing rat mEH, elaidamide enhances the toxicity effects of epoxide-containing xenobiotics. These inhibitors could be valuable tools for investigating the physiological and toxicological roles of mEH.

Method for sleep induction

Sleep may be induced by administration of fatty acid primary amides, including cis-9,10-octadecenoamide. Furthermore, sleep deprivation may be assayed by analyzing cerebrospinal fluid with respect to the presence of fatty acid primary amides, including cis-9,10-octadecenoamide. The presence of cis-9,10-octadecenoamide in cerebrospinal fluid is correlated with comparative sleep deprivation.