54738-27-1

Upstream product

• 54738-25-9 3,5-Dimethoxy-4-benzyloxy-β-carboxycinnamonitril 
• 294661-24-8 (E)-3-(4-Benzyloxy-3,5-dimethoxy-phenyl)-acrylonitrile 
• 6527-32-8 4-(benzyloxy)-3,5-dimethoxybenzaldehyde 
• 134-96-3 syringic aldehyde 

Downstream Products

• 54738-32-8 3-(3,5-dimethoxy-4-hydroxyphenyl)propylamine 
• 224564-34-5 3-benzyloxy-1-[3-(3,5-dimethoxy-4-hydroxyphenyl)propyl]-2-methyl-4(1H)-pyridinone 

Relevant academic research and scientific papers

Novel HIV-1 Non-nucleoside Reverse Transcriptase Inhibitor Agents: Optimization of Diarylanilines with High Potency against Wild-Type and Rilpivirine-Resistant E138K Mutant Virus

Three series (6, 13, and 14) of new diarylaniline (DAAN) analogues were designed, synthesized, and evaluated for anti-HIV potency, especially against the E138K viral strain with a major mutation conferring resistance to the new-generation non-nucleoside reverse transcriptase inhibitor drug rilpivirine (1b). Promising new compounds were then assessed for physicochemical and associated pharmaceutical properties, including aqueous solubility, log P value, and metabolic stability, as well as predicted lipophilic parameters of ligand efficiency, ligand lipophilic efficiency, and ligand efficiency-dependent lipophilicity indices, which are associated with ADME property profiles. Compounds 6a, 14c, and 14d showed high potency against the 1b-resistant E138K mutated viral strain as well as good balance between anti-HIV-1 activity and desirable druglike properties. From the perspective of optimizing future NNRTI compounds as clinical trial candidates, computational modeling results provided valuable information about how the R1 group might provide greater efficacy against the E138K mutant.

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.