54739-30-9

Usage

Uses

Used in Pharmaceutical Applications:
9(Z),11(E)-OCTADECADIENOIC ACID is used as a precursor for the production of biologically active compounds, such as 13-oxoODE, which has been found to stimulate cell proliferation and act as an activator of PPAR α (peroxisome proliferator-activated receptor α). This makes it a valuable compound in the development of pharmaceuticals targeting various health conditions.
Used in Nutritional Applications:
As an essential fatty acid, 9(Z),11(E)-OCTADECADIOENOIC ACID is used as a vital component in the human diet to support overall health and well-being. It is particularly important for maintaining healthy skin, hair, and nails, as well as for its role in the production of prostaglandins, which are involved in various physiological processes.
Used in the Food Industry:
9(Z),11(E)-OCTADECADIENOIC ACID is used as an ingredient in the food industry, particularly in the production of vegetable oils and margarines. Its presence in these products contributes to the overall health benefits of consuming a balanced diet rich in essential fatty acids.
Used in Cosmetic Applications:
Due to its beneficial properties for skin health, 9(Z),11(E)-OCTADECADIENOIC ACID is used as an ingredient in various cosmetic products, such as moisturizers, creams, and lotions. Its inclusion in these products helps to promote healthy skin and maintain its natural barrier function.

InChI:InChI=1/C18H30O3/c1-2-3-11-14-17(19)15-12-9-7-5-4-6-8-10-13-16-18(20)21/h7,9,12,15H,2-6,8,10-11,13-14,16H2,1H3,(H,20,21)/b9-7-,15-12+

Upstream product

• 60-33-3 linoleic acid 
• 79790-32-2 13-oxo-(9Z,11E)-octadecadien-1-oic acid methyl ester 
• 10219-69-9 (R,S)-coriolic acid 
• 33964-75-9 (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid 
• 60900-56-3 methyl 9Z,11E-13-hydroperoxyoctadecadienoate 
• 18320-18-8 13(S)-HpODE 
• 29623-28-7 (13S,9Z,11E)-13-hydroxy-9,11-octadecadienoic acid 
• 463-40-1 (9Z,12Z,15Z)-octadeca-9-12,15-trienoic acid 

Downstream Products

• 2389-06-2 13-oxooctadecanoic acid 
• 79790-32-2 13-oxo-(9Z,11E)-octadecadien-1-oic acid methyl ester 
• 2825-91-4 (R)-δ-decalactone 
• 6410-93-1 methyl coriolate 
• 2540-76-3 Methyl-13-hydroxystearat 
• 10219-69-9 (R,S)-coriolic acid 

Relevant academic research and scientific papers

The acid-promoted reaction of ethyl linoleate with nitrite. New insights from 15N-labelling and peculiar reactivity of a model skipped diene

The acid-promoted reaction of ethyl linoleate with nitrite ions was re-examined by an integrated approach based on the use of 15NO2- combined with extensive GC-MS (EI, NICI, PICI) and 2D 1H,15N and 1H,13C NMR analysis. The less polar products proved to be regioisomeric E-nitroalkenes, novel Z-nitroalkenes, and 3-nitro-1,5-hexadienes derivatives. A medium polarity fraction consisted mainly of stereo- and regioisomeric 1,2-nitronitrates along with 1,5-dinitro-1,3-pentadiene compounds. Novel 5-nitro-2,4-pentadienone products could be identified in the most polar fraction, which featured 1,2-nitroalcohols as the most abundant components. Under similar conditions 1,4-hexadiene gave mainly a nitrofuroxan derivative.

Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates

Bioactive oxylipins play multiple roles during inflammation and in the immune response, with termination of their actions partly dependent on the activity of yet-to-be characterized dehydrogenases. Here, we report that human microsomal dehydrogenase reductase 9 (DHRS9, also known as SDR9C4 of the short-chain dehydrogenase/reductase (SDR) superfamily) exhibits a robust oxidative activity toward oxylipins with hydroxyl groups located at carbons C9 and C13 of octadecanoids, C12 and C15 carbons of eicosanoids, and C14 carbon of docosanoids. DHRS9/SDR9C4 is also active toward lipid inflammatory mediator dihydroxylated Leukotriene B4 and pro-resolving mediators such as tri-hydroxylated Resolvin D1 and Lipoxin A4, although notably, with lack of activity on the 15-hydroxyl of prostaglandins. We also found that the SDR enzymes phylogenetically related to DHRS9, i.e., human SDR9C8 (or retinol dehydrogenase 16), the rat SDR9C family member known as retinol dehydrogenase 7, and the mouse ortholog of human DHRS9 display similar activity toward oxylipin substrates. Mice deficient in DHRS9 protein are viable, fertile, and display no apparent phenotype under normal conditions. However, the oxidative activity of microsomal membranes from the skin, lung, and trachea of Dhrs9?/? mice toward 1 μM Leukotriene B4 is 1.7- to 6-fold lower than that of microsomes from wild-type littermates. In addition, the oxidative activity toward 1 μM Resolvin D1 is reduced by about 2.5-fold with DHRS9-null microsomes from the skin and trachea. These results strongly suggest that DHRS9 might play an important role in the metabolism of a wide range of bioactive oxylipins in vivo.

Catalytic production of oxo-fatty acids by lipoxygenases is mediated by the radical-radical dismutation between fatty acid alkoxyl radicals and fatty acid peroxyl radicals in fatty acid assembly

Oxo-octadecadienoic acids (OxoODEs) act as peroxisome proliferator-activated receptor (PPAR) agonists biologically, and are known to be produced in the lipoxygenase/linoleate system. OxoODEs seem to originate from the linoleate alkoxyl radicals that are generated from (E/Z)-hydroperoxy octadecadienoic acids ((E/Z)HpODEs) by a pseudoperoxidase reaction that is catalyzed by ferrous lipoxygenase. However, the mechanism underlying the conversion of alkoxyl radical into OxoODE remains obscure. In the present study, we confirmed that OxoODEs are produced in the lipoxygenase/linoleate system in an oxygen-dependent manner. Interestingly, we revealed a correlation between the (E/Z)-OxoODEs content and the (E/E)-HpODEs content in the system. (E/E)-HpODEs could have been derived from (E/E)-linoleate peroxyl radicals, which are generated by the reaction between a free linoleate allyl radical and an oxygen molecule. Notably, the ferrous lipoxygenase-linoleate allyl radical (LOx(Fe2+)-L·) complex, which is an intermediate in the lipoxygenase/linoleate system, tends to dissociate into LOx(Fe2+) and a linoleate allyl radical. Subsequently, LOx(Fe2+) converts (E/Z)-HpODEs to an (E/Z)-linoleate alkoxyl radical through one-electron reduction. Taken together, we propose that (E/Z)-OxoODEs and (E/E)-HpODEs are produced through radical-radical dismutation between (E/Z)-linoleate alkoxyl radical and (E/E)-linoleate peroxyl radical. Furthermore, the production of (E/Z)OxoODEs and (E/E)-HpODEs was remarkably inhibited by a hydrophobic radical scavenger, 2,2,6,6-tetra-methylpiperidine 1-oxyl (TEMPO). On the contrary, water-miscible radical scavengers, 4-hydroxyl-2,2,6,6-tetramethylpiperidine 1-oxyl (OH-TEMPO) and 3-carbamoyl-2,2,5,5-tetramethyl-3-pyrroline-N-oxyl (CmΔP) only modestly or sparingly inhibited the production of (E/Z)-OxoODEs and (E/E)-HpODEs. These facts indicate that the radical-radical dismutation between linoleate alkoxyl radical and linoleate peroxyl radical proceeds in the interior of micelles.

Oxidation of C18 Hydroxy-Polyunsaturated Fatty Acids to Epoxide or Ketone by Catalase-Related Hemoproteins Activated with Iodosylbenzene

Small catalase-related hemoproteins with a facility to react with fatty acid hydroperoxides were examined for their potential mono-oxygenase activity when activated using iodosylbenzene. The proteins tested were a Fusarium graminearum 41?kD catalase hemoprotein (Fg-cat, gene FGSG_02217), a Pseudomonas fluorescens Pfl01 catalase (37.5?kD, accession number WP_011333788.1), and a Mycobacterium avium ssp. paratuberculosis 33?kD catalase (gene MAP-2744c). 13-Hydroxy-octadecenoic acids (which are normally unreactive) were selected as substrates because these enzymes react specifically with the corresponding 13S-hydroperoxides (Pakhomova et al. 18:2559–2568, 5; Teder et al. 1862:706–715, 14). In the presence of iodosylbenzene Fg-cat converted 13S-hydroxy-fatty acids to two products: the 15,16-double bond of 13S-hydroxy α-linolenic acid was oxidized stereospecifically to the 15S,16R-cis-epoxide or the 13-hydroxyl was oxidized to the 13-ketone. Products were identified by UV, HPLC, LC–MS, NMR and by comparison with authentic standards prepared for this study. The Pfl01-cat displayed similar activity. MAP-2744c oxidized 13S-hydroxy-linoleic acid to the 13-ketone, and epoxidized the double bonds to form the 9,10-epoxy-13-hydroxy, 11,12-epoxy-13-hydroxy, and 9,10-epoxy-13-keto derivatives; equivalent transformations occurred with 9S-hydroxy-linoleic acid as substrate. In parallel incubations in the presence of iodosylbenzene, human catalase displayed no activity towards 13S-hydroxy-linoleic acid, as expected from the highly restricted access to its active site. The results indicated that with suitable transformation to Compound I, monooxygenase activity can be demonstrated by these catalase-related hemoproteins with tyrosine as the proximal heme ligand.

Macamides compound and synthetic method and application thereof

The invention relates to the field of drugs, in particular to a macamides compound and a synthetic method and application thereof. The synthetic method of macamides comprises the steps that linoleic acid and an oxidizing agent are subjected to catalytic oxidation through pyridine derivatives to obtain a macaenes mixture; the macaenes mixture and benzylamine or benzylamine derivatives are subjected to amidation and then separated through preparative chromatography, wherein the oxidizing agent is one of 2,2,6,6-tempol-nitrogen-oxide, pyridinium tribromide, 2-Iodoxybenzoic acid; the benzylamine derivatives are 3-trimethoprim or 3,4-dimethoxybenzamine. Linoleic acid is adopted as a starting reactant to be synthesized, and compared with the prior art that mecamide is extracted from plant maca, the needed raw material is low in cost and easy to obtain; in addition, in the synthesis preparation process, operation is easy, few by-products are produced, the needed reagents and solvents are small in toxicity and easy to obtain, and the novel path is provided for preparing a large number of macamides monomeric compounds.

Inhibitory and mechanistic investigations of oxo-lipids with human lipoxygenase isozymes

Oxo-lipids, a large family of oxidized human lipoxygenase (hLOX) products, are of increasing interest to researchers due to their involvement in different inflammatory responses in the cell. Oxo-lipids are unique because they contain electrophilic sites that can potentially form covalent bonds through a Michael addition mechanism with nucleophilic residues in protein active sites and thus increase inhibitor potency. Due to the resemblance of oxo-lipids to LOX substrates, the inhibitor potency of 4 different oxo-lipids; 5-oxo-6,8,11,14-(E,Z,Z,Z)-eicosatetraenoic acid (5-oxo-ETE), 15-oxo-5,8,11,13-(Z,Z,Z,E)-eicosatetraenoic acid (15-oxo-ETE), 12-oxo-5,8,10,14-(Z,Z,E,Z)-eicosatetraenoic acid (12-oxo-ETE), and 13-oxo-9,11-(Z,E)-octadecadienoic acid (13-oxo-ODE) were determined against a library of LOX isozymes; leukocyte 5-lipoxygenase (h5-LOX), human reticulocyte 15-lipoxygenase-1 (h15-LOX-1), human platelet 12-lipoxygenase (h12-LOX), human epithelial 15-lipoxygenase-2 (h15-LOX-2), soybean 15-lipoxygenase-1 (s15-LOX-1), and rabbit reticulocyte 15-LOX (r15-LOX). 15-Oxo-ETE exhibited the highest potency against h12-LOX, with an IC50 = 1 ± 0.1 μM and was highly selective. Steady state inhibition kinetic experiments determined 15-oxo-ETE to be a mixed inhibitor against h12-LOX, with a Kic value of 0.087 ± 0.008 μM and a Kiu value of 2.10 ± 0.8 μM. Time-dependent studies demonstrated irreversible inhibition with 12-oxo-ETE and h15-LOX-1, however, the concentration of 12-oxo-ETE required (Ki = 36.8 ± 13.2 μM) and the time frame (k2 = 0.0019 ± 0.00032 s-1) were not biologically relevant. These data are the first observations that oxo-lipids can inhibit LOX isozymes and may be another mechanism in which LOX products regulate LOX activity.

Quantitation of hydroperoxy-, keto- and hydroxy-dienes during oxidation of FAMEs from high-linoleic and high-oleic sunflower oils

The objective of this work was to study the quantitative formation of hydroperoxydienes, ketodienes and hydroxydienes during autoxidation at 40 °C of fatty acid methyl esters derived from two sunflower oils with different degree of unsaturation, high-linoleic sunflower oil and high-oleic sunflower oil. The analysis of the oxidation compounds was carried out by NP-HPLC-UV and results were compared to the specific extinction at 232 nm (K 232) and the peroxide value (PV). Analysis of FAME polymers by HPSEC was also performed to discard samples of advanced oxidation. Results showed that the contents of hydroperoxydienes with respect to the PV were higher for the high linoleic (HL) sample. At the end of the period of slow polymerization (ΔPol ≤ 1 wt%), the content of hydroperoxydienes was found to be 86.0 and 30.7 μg/mg for the HL and high oleic (HO) samples, respectively. Throughout this period, hydroperoxydienes constituted around 90 and 50 wt% of the total hydroperoxides in the HL and HO samples, respectively, suggesting that a significant oxidation of oleic acid also occurred in both samples. The contents of ketodienes and hydroxydienes as a whole constituted 2-3 wt% of the diene compounds analyzed at the end of the period of slow polymerization. Higher contents of ketodienes than of hydroxydienes were found throughout the oxidation time, and the ratio between the contents of ketodienes and hydroxydienes increased with a factor that changed from 1 to 2 throughout the period of slow polymerization.

Physcomitrella patens has lipoxygenases for both eicosanoid and octadecanoid pathways

Mosses have substantial amounts of long chain C20 polyunsaturated fatty acids, such as arachidonic and eicosapentaenoic acid, in addition to the shorter chain C18 α-linolenic and linoleic acids, which are typical substrates of lipoxygenases in flowering p

Free radical oxidation of coriolic acid (13-(S)-hydroxy-9Z,11E- octadecadienoic acid)

The reaction of (13S,9Z,11E)-13-hydroxy-9,11-octadecadienoic acid (1a), one of the major peroxidation products of linoleic acid and an important physiological mediator, with the Fenton reagent (Fe2+/EDTA/H 2O2) was investigated. In phosphate buffer, pH 7.4, the reaction proceeded with >80% substrate consumption after 4 h to give a defined pattern of products, the major of which were isolated as methyl esters and were subjected to complete spectral characterization. The less polar product was identified as (9Z,11E)-13-oxo-9,11-octadecadienoate (2) methyl ester (40% yield). Based on 2D NMR analysis the other two major products were formulated as (11E)-9,10-epoxy-13-hydroxy-11-octadecenoate (3) methyl ester (15% yield) and (10E)-9-hydroxy-13-oxo-10-octadecenoate (4) methyl ester (10% yield). Mechanistic experiments, including deuterium labeling, were consistent with a free radical oxidation pathway involving as the primary event H-atom abstraction at C-13, as inferred from loss of the original S configuration in the reaction products. Overall, these results provide the first insight into the products formed by oxidation of 1a with the Fenton reagent, and hint at novel formation pathways of the hydroxyepoxide 3 and hydroxyketone 4 of potential (patho)physiological relevance in settings of oxidative stress.

Characterization and quantification of free and esterified 9- and 13-hydroxyoctadecadienoic acids (HODE) in barley, germinating barley, and finished malt

The analysis of (R)-9- and (S)-9-hydroxy-10E,12Z-octadecadienoic acid as well as (R)-13- and (S)-13-hydroxy-9Z,11E-octadecadienoic acid (HODE) as free acids, esterified in triacylglycerols (storage lipids), and esterified in polar lipids (phospholipids, glycolipids, etc.) in barley, germinating barley, and finished malt was performed using [13-18O1]-(S)-13-HODE isotope dilution assays with GC-MS and straight- and chiral-phase HPLC. 9- and 13-HODE occur approximately racemically in barley, indicating an autoxidation. The enantiomeric excesses increase to 78% S for free 9-HODE and to 58% S for free 13-HODE in germinating barley as a result of lipoxygenase-2 (LOX-2) catalysis, but free HODEs are at low concentration. More than 90% of HODEs in barley and malt are esterified. In the storage lipids of green malt 53 mg/kg 9-HODE and 147 mg/kg 13-HODE were detected. This ratio of 30:70 reflects the regioselectivity of the LOX-2 enzyme in malt. In the polar lipids 45 mg/kg 9-HODE and 44 mg/kg 13-HODE were characterized. The latter indicate a hitherto unknown 9-lipoxygenase activity with polar lipids as substrates. During kilning the contents of most HODEs decreased significantly due to chemical and enzymatic degradation, whereas polar-esterified (R)-13-HODE increased (43%) in the finished malt.