131138-14-2

Upstream product

• 1198777-94-4 tert-butyl{(R)-1-[(R)-oxiran-2-yl]heptyloxy}diphenylsilane 

Downstream Products

• 121644-19-7 5-[(1S,2R)-2-(tert-Butyl-diphenyl-silanyloxy)-1-methyl-octyl]-2,2-dimethyl-[1,3]dioxane-4,6-dione 
• 121644-01-7 5-[(R)-2-(tert-Butyl-diphenyl-silanyloxy)-octylidene]-2,2-dimethyl-[1,3]dioxane-4,6-dione 

Relevant academic research and scientific papers

Total synthesis of mycestericin A and its 14-epimer

The total synthesis of mycestericin A (1) and its 14-epimer 34 is described herein. The Overman rearrangement of an allylic trichloroacetimidate derived from l-tartrate generated a tetra-substituted carbon with nitrogen and subsequent stereoselective transformations afforded the highly functionalized left-half segment, vinyl iodide. Cross-coupling of the vinyl iodide with a chiral organometallic species synthesized from d-tartrate under the Negishi or Suzuki-Miyaura coupling conditions, followed by deprotection, completed the total synthesis of 1. The 14-epimer of mycestericin A was also synthesized, and a comparison of [α]D values of peracetyl γ-lactone derivatives of mycestericin A and its 14-epimer as well as degradation studies of 1 and 34 fully confirmed the proposed absolute structure of mycestericin A.

Synthesis of two analogues of Arachidonic Acid and their reactions with 12-lipoxygenase

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.