194715-64-5

Upstream product

• 105480-73-7 (β-ionyl)triphenylphosphonium bromide 
• 135414-23-2 (9Z)-11-methylretinal 
• 859773-36-7 1,3-dimethyl-5-(2,6,6-trimethylcyclohexa-1-enyl)penta-2,4-dien-1-ol 
• 1266619-29-7 11-methylretinonitrile 
• 3917-41-7 (2E,4E)-3-methyl-5-(2,6,6-trimethyl-1-cyclohexen-1-yl)-2,4-pentadienal 
• 138846-06-7 2-[(1’E,3’E)-3’-methyl-4’-iodobuta-1’,3’-dien-1’yl]-1,3,3-trimethylcyclohex-1-ene 
• 154547-39-4 (E)-3-methylhex-2-en-4-yn-1-ol 
• 154547-38-3 (E)-tert-butyldimethyl((3-methylhex-2-en-4-yn-1-yl)oxy)silane 
• 121693-79-6 (E)-tert-butyldimethyl-((3-methylpent-2-en-4-yn-1-yl)oxy)silane 
• 6153-06-6 (E)-3-methylpent-2-en-4-yn-1-ol 
• 79-77-6 (E)-β-ionone 

Relevant academic research and scientific papers

Synthesis of C11-to-C14 methyl-shifted all-: Trans -retinal analogues and their activities on human aldo-keto reductases

Human aldo-keto reductases (AKRs) are enzymes involved in the reduction, among other substrates, of all-trans-retinal to all-trans-retinol (vitamin A), thus contributing to the control of the levels of retinoids in organisms. Structure-activity relationship studies of a series of C11-to-C14 methyl-shifted (relative to natural C13-methyl) all-trans-retinal analogues as putative substrates of AKRs have been reported. The synthesis of these retinoids was based on the formation of a C10-C11 single bond of the pentaene skeleton starting from a trienyl iodide and the corresponding dienylstannanes and dienylsilanes, using the Stille-Kosugi-Migita and Hiyama-Denmark cross-coupling reactions, respectively. Since these reagents differ by the location and presence of methyl groups at the dienylorganometallic fragment, the study also provided insights into the ability of the different positional isomers to undergo cross-coupling and the sensitivity of these processes to steric hindrance. The resulting C11-to-C14 methyl-shifted all-trans-retinal analogues were found to be active substrates when tested with AKR1B1 and AKR1B10 enzymes, although relevant differences in substrate specificities were noted. For AKR1B1, all analogues exhibited higher catalytic efficiency (kcat/Km) than parent all-trans-retinal. In addition, only all-trans-11-methylretinal, the most hydrophobic derivative, showed a higher value of kcat/Km = 106 000 ± 23 200 mM-1 min-1 for AKR1B10, which is in fact the highest value from all known retinoid substrates of this enzyme. The novel structures, identified as efficient AKR substrates, may serve in the design of selective inhibitors with potential pharmacological interest. This journal is

Efficient preparation of 9-Z-11-methylretinal and 11-Z-11-methylretinal

[2-(β-Ionylidene)propyl]triphenylphosphonium bromide is reacted with 3-methyl-4-oxobut-2-enenitrile in refluxing 1,2-epoxybutane to give a mixture of 11-Z- and all-E-11-methylretinal via DIBAL-H reduction. In an analogous fashion, β-ionyl triphenylphospho

Unusual conformation and photoisomerization of retinochrome analogues with 11-methylretinals

Three kinds of 11-methylretinals were synthesized for elucidating effect of methyl substitution on formation of retinochrome-analogues and their properties. The stable conformation of 11-methylretinal was found as 6,10,12-tri-S-cis conformation based on NOESY measurement. The formed retinochrome-analogues with 11-Me-, 11-Me-13-deMe-and 11-Me-9,13-dideMe-retinals showed their absorption maxima at 450, 470 and 470 nm, respectively. The enzymatic photoisomerization of their retinochrome-analogues gave the 11-cis isomers in 90-91 % regioselectivity. The CD spectra of 11-methylretinochrome exhibited the intense β-band with extremely weak α-band.