50604-10-9

Upstream product

• 50604-12-1 methyl p-(1-hydroxy-1-methylethyl)benzoate 
• 67-56-1 methanol 
• 26581-23-7 4-(1-methylethenyl)benzoic acid methyl ester 
• 3609-50-5 4-(2-hydroxypropan-2-yl)benzoic acid 
• 74-88-4 methyl iodide 
• 619-58-9 4-iodobenzoic acid 

Downstream Products

• 50604-11-0 4-(1-methoxy-1-methylethyl)benzoic acid 

Relevant academic research and scientific papers

INFLUENZA VIRUS INHIBITOR TARGETING NUCLEOPROTEIN

This document discloses a novel class of compound for treating influenza A and influenza B viral infection, and compositions and methods of use thereof.

Proline-Rich Short Peptides with Photocatalytic Activity for the Nucleophilic Addition of Methanol to Phenylethylenes

Short proline-rich peptides were synthesized and modified with 1-(N,N-dimethylamino)pyrene by copper(I)-catalyzed cycloaddition. They perform photoredox catalysis of the nucleophilic addition of methanol to 1,1-diphenylethylene derivatives into products with Markovnikov orientation. The common additive triethylamine is avoided because forward and backward electron transfer is controlled by substrate binding. A free carboxylic function in the substrate allows more precise substrate binding and defines the electron transfer path better than the unspecific exciplex formation with the substrate bearing a carboxylic ester. A proline-type turn is an advantage for photoredox catalysis, but a proline-induced helix is not required. This is the first successful example for introducing secondarily structured peptides to photoredox catalysis.

MODULATORS OF METHYL MODIFYING ENZYMES, COMPOSITIONS AND USES THEREOF

Agents for modulating methyl modifying enzymes, compositions and uses thereof are provided herein.

MODULATORS OF METHYL MODIFYING ENZYMES, COMPOSITIONS AND USES THEREOF

Agents for modulating methyl modifying enzymes, compositions and uses thereof are provided herein.

Antithrombotic agents

This application relates to a compound of formula (I), a pharmaceutically acceptable salt of the compound, or a prodrug thereof, as defined herein, pharmaceutical compositions thereof, and its use as an inhibitor of factor Xa, as well as a process for its preparation and intermediates therefor.

1,2-Dibenzamidobenzene inhibitors of human factor Xa

High-throughput screening of a combinatorial library of diamidophenols yielded lead compounds with the ability to inhibit human factor Xa (fXa) at micromolar concentrations (e.g. compound 4, fXa apparent K(ass) = 0.64 x 106 L/mol). SAR studies in this novel structural series of fXa inhibitors showed that the phenolic hydroxyl group was not essential for activity. The best activity was found in substituted 1,2-dibenzamidobenzenes in which the phenyl group of one benzoyl group (A-ring) was substituted in the 4-position with relatively small lipophilic or polarizable groups such as methoxy, vinyl, or chloro and the phenyl group of the other benzoyl group (B-ring) was substituted in the 4-position with larger lipophilic groups such as tertbutyl or dimethylamino. The central phenyl ring (C-ring) tolerated a wide variety of substituents, but methoxy, methanesulfonamido, hydroxyl, and carboxyl substitution produced slightly higher levels of activity than other substituents when present in combination with favorable B-ring substitution. Methylation of the amide nitrogen atoms was found to greatly decrease activity. Compound 12 is the highest affinity fXa inhibitor in this group of compounds, having fXa apparent K(ass) = 25.5 x 106 L/mol, about 40x more active than the original lead. This lead series does not show potent inhibition of human thrombin. A model for the binding of these ligands to the fXa active site is proposed. The model is consistent with the observed SAR and can serve to guide future SAR studies.