117458-66-9Relevant academic research and scientific papers
Synthesis of resolvin E3 via palladium-catalyzed addition of AcOH to vinyl epoxy alcohols
Tanabe, Shuhei,Kobayashi, Yuichi
, p. 2393 - 2402 (2019)
(18R)- and (18S)-stereoisomers of resolvin E3 (RvE3), potent anti-inflammatory mediators, were synthesized stereo- and enantioselectively through the Wittig reaction of the carbonate of 6R,7R- and 6R,7S-dihydroxynona-2E,4E-dienal, a C12-C20 part, with the
Novel, potent THC/anandamide (hybrid) analogs
Bourne, Caryl,Roy, Sucharita,Wiley, Jenny L.,Martin, Billy R.,Thomas, Brian F.,Mahadevan, Anu,Razdan, Raj K.
, p. 7850 - 7864 (2008/04/12)
The structure-activity relationship (SAR) of the end pentyl chain in anandamide (AEA) has been established to be very similar to that of Δ9-tetrahydrocannabinol (Δ9-THC). In order to broaden our understanding of the structural similarities between AEA and THC, hybrid structures 1-3 were designed. In these hybrids the aromatic ring of THC-DMH was linked to the AEA moiety through an ether linkage with the oxygen of the phenol of THC. Hybrid 1 (O-2220) was found to have very high binding affinity to CB1 receptors (Ki = 8.5 nM), and it is interesting to note that the orientation of the side chain with respect to the oxygen in the phenol is the same as in THCs. To further explore the SAR in this series the terminal carbon of the side chain was modified by adding different substituents. Several such analogs were synthesized and tested for their CB1 and CB2 binding affinities and in vivo activity (tetrad tests). The details of the synthesis and the biological activity of these compounds are described.
Synthesis of two analogues of Arachidonic Acid and their reactions with 12-lipoxygenase
Labelle, Marc,Falgueyret, Jean-Pierre,Riendeau, Denis,Rokach, Joshua
, p. 6301 - 6310 (2007/10/02)
Two analogues of arachidonic acid (AA) were synthesized and their reaction with purified porcine 12-lipoxygenase was investigated. The analogue (Z,Z,Z,E)-5,8,11,13 eicosatetraienoic acid 1 was found to be a substrate for the enzyme, being oxidized at one third the rate of AA. The structure of the lipoxygenation product, as well as its absolute stereochemistry, were determined by comparison of the enzymatic reaction product with a synthetic sample of known stereochemistry, prepared from L-arabinose. The oxygenation of 1 by 12-lipoxygenase occurred selectively at carbon 14 and yielded only the S-isomer. The second AA analogue (Z,Z,Z,E,E)-5,8,11,13,15 eicosapentaenoic acid 2 failed to give any detectable amount of product upon incubation with the enzyme. The results demonstrate that the 15-oxygenated function of 15-H(P)ETE is not a requirement for the stereoselective 14-oxygenation catalyzed by 12-lipoxygenase. Furthermore, these results support the proposal that AA binds in a horseshoe like conformation at the active site of lipoxygenase.
