178167-77-6

Usage

InChI:InChI=1/C15H20O3/c1-10-4-5-12-6-8-15(3,9-7-13(16)17)18-14(12)11(10)2/h4-5H,6-9H2,1-3H3,(H,16,17)

Upstream product

• 1073-11-6 5-methyl-5-vinyl-dihydro-furan-2-one 
• 526-75-0 2,3-Dimethylphenol 
• 109-63-7 trifluoroborane diethyl ether 

Relevant academic research and scientific papers

Use of gamma -tocopherol and its oxidative metabolite LLU- alpha in the treatment of natriuretic disease

The present invention is generally related to the discovery of the therapeutic benefit of administering gamma -tocopherol and gamma -tocopherol derivatives. More specifically, the use of gamma -tocopherol and racemic LLU- alpha , (S)-LLU- alpha , or gamma -tocopherol derivatives as antioxidants and nitrogen oxide scavengers which treat and prevent high blood pressure, thromboembolic disease, cardiovascular disease, cancer, natriuretic disease, the formation of neuropathological lesions, and a reduced immune system response are disclosed.

Endogenous natriuretic factors 6: The stereochemistry of a natriuretic γ-tocopherol metabolite LLU-α

2,7,8-Trimethyl-(S)-2-(β-carboxyethyl)-6-hydroxy chroman (S-LLU-α) isolated from human uremic urine is apparently an oxidative side-chain degradation product of γ-tocopherol. This compound exhibits natriuretic activity in vivo and it appears to mediate the inhibition of the 70 pS K+ channel in the apical membrane of the thick ascending limb of the nephron. The stereochemistry at the C-2 of LLU-α has been unequivocally established to be S(+) by X-ray crystallographic analysis of a diastereomeric amide derivative. It was also established that the chroman ring oxidation of S- LLU-α proceeded without racemization at C-2. This finding can be extended to nonepimerization at C-2 of α-δ tocopherols (Vitamin E) during side-chain oxidation and stereospecificity (retention or inversion) of oxidative opening of the chroman ring. The resolution of the enantiomers of the parent compound and derivatives was accomplished by chiral high-performance liquid chromatography. The stereospecific enzymatic hydrolysis by an array of commercially available enzymes of the racemic methyl ester of LLU-α was investigated. The lipase from Humicola languinosa appears to be the best enzyme for resolution by selective hydrolysis of the racemic methyl ester.