2176-16-1

Upstream product

• 6527-33-9 4-benzyloxy-3,5-dimethoxy-β-nitrostyrene 
• 6527-33-9 2-(benzyloxy)-1,3-dimethoxy-5-(2-nitroethenyl)benzene 
• 134-96-3 syringic aldehyde 
• 42973-55-7 4-hydroxy-3,5-dimethoxyphenylacetonitrile 
• 100-39-0 benzyl bromide 
• 27065-65-2 methyl 4-benzyloxy-3,5-dimethoxybenzoate 
• 100-44-7 benzyl chloride 
• 14588-60-4 4-(benzyloxy)-3,5-dimethoxybenzoic acid 
• 530-57-4 3,5-dimethoxy-4-hydroxybenzoic acid 
• 2176-18-3 4-benzyloxy-3,5-dimethoxybenzyl alcohol 
• 6527-32-8 4-(benzyloxy)-3,5-dimethoxybenzaldehyde 
• 2176-17-2 4-benzyloxy-3,5-dimethoxyphenylacetonitrile 

Downstream Products

• 224564-33-4 3-benzyloxy-1-[2-(4-benzyloxy-3,5-dimethoxyphenyl)ethyl]-2-methyl-4(1H)-pyridinone 

Relevant academic research and scientific papers

A process for preparing a broad pH fluorescent probe of the organic compound and use thereof (by machine translation)

The present invention discloses a process for the preparation of a wide range of fluorescent probe in the pH of the organic compound, the organic compound can be produced according to the actual need to carry out any proportion of combination, and can be fixed in the hydrophilic high polymer further preparing and detecting water environment acidity and alkalinity of the product. The product can be realized to the pH value of the continuous measuring, thereby greatly improving the efficiency, sensitivity and repeatability. (by machine translation)

Biosynthesis. Part 24. Speculative Incorporation Experiments with 1-Benzylisoquinolines and a Logical Approach via C6-C2 and C6-C3 Precursors to the Biosynthesis of Hasubanonine and Protostephanine

Many possible 1-benzyltetrahydroisoquinolines have been examined as possible advanced precursors of the alkaloids hasubanonine (1) and protostephanine (2) in Stephania japonica plants, but none was incorporated significantly.Administration of various precursor molecules having only one aromatic ring, such as tyrosine, has demonstrated that both alkaloids are derived from two different C6-C2 biogenetic units.The subsequent failure of further 1-benzyltetrahydroisoquinolines and bisphenethylamines to be incorporated suggested the intermediacy of either (a) modified 1-benzylisoquinolines or (b) trioxygenated C6-C2 building blocks.Precursors designed to examine the first possibility, such as 1-benzyl-3,4-dihydroisoquinolines or 1-benzyl-1-carboxytetrahydroisoquinolines, were not incorporated into (1) and (2) whereas two 3',4',5'-trioxygenated 2-phenylethylamines were incorporated.These findings allow further delineation of the requirements for later precursors of the alkaloids (1) and (2).

Lipophilicity and serotonin agonist activity in a series of 4 substituted mescaline analogues

Replacement of the 4 methoxy of mescaline with higher alkyl homologues or with bromine led to increased activity at serotonin receptors in a sheep umbilical artery preparation. This activity appears correlated with lipophilicity, as measured by 1 octanol water partition coefficients, but drops off when the 4 substituent is about five atoms in length. It is suggested that 3,4,5 trisubstitution may give compounds which are as active as those with the 2,4 5 substitution pattern.

Catechol O methyltransferase. VI. Affinity labeling with N haloacetyl 3,5 dimethoxy 4 hydroxyphenylalkylamines

Several N acyl 4 hydroxy 3,5 dimethoxy phenylalkylamines were synthesized and evaluated for ability to inactivate catechol O methyltransferase (COMT). 4 Hydroxy N iodoacetyl 3,5 dimethoxy phenylethylamine was found to rapidly and irreversibly inactivate this enzyme. The corresponding n concentrations bromoacetyl derivative also produced inactivation of COMT but at a slower rate than the N iodoacetyl derivative. The N acetyl and N fumaryl derivatives were completely inactive. Inactivation of COMT by these reagents appears to proceed by a unimolecular reaction within a dissociable complex rather than by a nonspecific bimolecular reaction. The proximity of the amino acid residue being modified relative to the site which binds the aromatic portion of these inhibitors was determined using N iodoactylphenylalkylamines of varying chain length. The number of methylene carbons separating the aromatic ring and the iodoacetamide moiety in these inhibitors did not greatly influence the binding to COMT nor did it affect how rapidly the enzyme was inactivated. From these observations it is concluded that the amino acid moiety being modified by this class of affinity labeling reagents must be relatively close to or part of the site which binds the aromatic region of these inhibitors.