10335-69-0

Basic information

• Product Name: OLEYLHYDROXAMIC ACID
• Synonyms: OLEYLHYDROXAMIC ACID;N-hydroxyoleamide;(9Z)-9-Octadecenehydroxamic acid;(Z)-N-Hydroxy-9-octadecenamide;Hydroxamate derivative of oleic acid;N-Hydroxyoleic amide;Oleoylhydroxamic acid;9-Octadecenamide, N-hydroxy-, (9Z)-
• CAS NO: 10335-69-0
• Molecular Formula: C₁₈H₃₅NO₂
• Molecular Weight: 297.48
• EINECS: 233-728-4
• Mol File: 10335-69-0.mol
• Article Data: 9

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 0.921g/cm³
• Refractive Index: 1.473
• Solubility: ≤50mg/ml in ethanol;50mg/ml in DMSO;50mg/ml in dimethyl formamide
• CAS DataBase Reference: OLEYLHYDROXAMIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: OLEYLHYDROXAMIC ACID(10335-69-0)
• EPA Substance Registry System: OLEYLHYDROXAMIC ACID(10335-69-0)

Safety Data

• Hazardous Substances Data: 10335-69-0(Hazardous Substances Data)

Usage

Biological Activity

mmp-2 inhibitor i, a hydroxamate-based, long-chain fatty acid, is a reversible inhibitor of matrix metalloproteinase (mmp)-2.matrix metalloproteinases (mmps) have been involved in the degradation of extracellular matrix. mmps contribute to long-term remodeling processes such as embryogenesis, tumor invasion, inflammation, angiogenesis, and wound healing. mmp-2, also known as gelatinase a or type iv collagenase, has been involved in regulating diverse cellular functions independent of its action on the extracellular matrix, including vascular tone, platelet aggregation, and mediation of the acute mechanical dysfunction of the heart immediately after ischemia and reperfusion [2]. up-regulation of mmp-2 has been associated with tumor invasion and metastasis [3].mmp-2 inhibitor i inhibited the activity of matrix metalloproteinase (mmp)-2 with the ki value of 1.6 μm [1]. mmp-2 inhibitor i attenuated cancer cell migration [3]. mmp-2 inhibitor i had also been used to preserve blood-brain barrier function in a wistar rat model of pneumococcal meningitis [4].

references

[1] berton a, rigot v, huet e, et al. involvement of fibronectin type ii repeats in the efficient inhibition of gelatinases a and b by long-chain unsaturated fatty acids[j]. journal of biological chemistry, 2001, 276(23): 20458-20465.[2] wang w, schulze c j, suarez-pinzon w l, et al. intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury[j]. circulation, 2002, 106(12): 1543-1549.[3] emmert-buck m r, roth m j, zhuang z, et al. increased gelatinase a (mmp-2) and cathepsin b activity in invasive tumor regions of human colon cancer samples[j]. the american journal of pathology, 1994, 145(6): 1285.[4] barichello t, generoso j s, michelon c m, et al. inhibition of matrix metalloproteinases-2 and-9 prevents cognitive impairment induced by pneumococcal meningitis in wistar rats[j]. experimental biology and medicine, 2014, 239(2): 225-231.

InChI:InChI=1/C18H35NO2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(20)19-21/h9-10,21H,2-8,11-17H2,1H3,(H,19,20)/b10-9-

Upstream product

• 111-62-6 oleic acid ethyl ester 
• 122-32-7 trioleoylglycerol 
• 112-77-6 (Z)-9-octadecenoyl chloride 
• 79-37-8 oxalyl dichloride 
• 112-80-1 cis-Octadecenoic acid 
• 112-62-9 Methyl oleate 
• 6114-18-7 elaidic acid ethyl ester 
• 64833-92-7 oleoylimidazole 

Downstream Products

• 112-79-8 Elaidic acid 
• 1610968-09-6 benzyl N-[(8Z)-heptadec-8-en-1-yl]carbamate 

Relevant articles and documents

Design, synthesis and CoMFA studies of OEA derivatives as FAAH inhibitors

A total of 26 novel oleoylethanolamide derivatives were designed, synthesized, and characterized. All synthesized targets compounds were screened for their inhibitory activities against fatty acid amide hydrolase. Among of them, 13 compounds inhibit fatty acid amide hydrolase by 50% at the concentration of 100 μM. Of these compounds, the most active one is compound 9, which inhibit fatty acid amide hydrolase activity 98.35% at the concentration of 100 μM. Comparative molecular field analysis analyzes were performed based on obtained biological activities data and resulted in a statistically reliable comparative molecular field analysis model with high predictive abilities (r2 = 0.978, q2 = 0.613).

An Environmentally Sustainable Mechanochemical Route to Hydroxamic Acid Derivatives

An operationally simple, and cost efficient conversion of carboxylic acids into hydroxamic acid derivatives via a high-energy mechanochemical activation is presented. This ball milling methodology was applied to a wide variety of carboxylic acids dramatically improving purification issues associated with this class of molecules, which still remain one of the main bottlenecks of classical methodologies. (Figure presented.).

Introducing catalytic lossen rearrangements: Sustainable access to carbamates and amines

A new, highly efficient and environmentally benign catalytic variant of the Lossen rearrangement is described. Dimethyl carbonate (DMC) as green activation reagent of hydroxamic acids in presence of catalytic amounts of tertiary amine bases {1,5,7-triazabicyclo[4.4.0]dec-5-ene (TBD), 1,8-biazabicyclo 5.4.0 undec-7-ene (DBU), 1,4-diazabicyclo[2.2.2]octane (DABCO), and triethylamine} and small quantities of methanol initiate the rearrangement. Methyl carbamates were obtained in good to moderate yields when aliphatic hydroxamic acids were employed in this catalytic Lossen rearrangement; under the same conditions aromatic hydroxamic acids yielded anilines. Notably, the mixture of DMC/methanol was recycled several times without observing decreased yields, thus minimizing the produced waste. Moreover, several other organic carbonates were successfully employed in the introduced catalytic Lossen rearrangement procedure. Copyright