14352-58-0

Usage

Uses

Used in Pharmaceutical Industry:
(1-methylcyclohexyl)acetic acid is used as an IRE1 modulator for the treatment of IRE1-related diseases. IRE1 (Inositol-requiring enzyme 1) is a type of protein that plays a crucial role in the unfolded protein response (UPR) and is associated with various diseases, including neurodegenerative disorders and certain types of cancer. By modulating the activity of IRE1, (1-methylcyclohexyl)acetic acid can potentially help in the development of therapeutic strategies to combat these conditions.

Upstream product

• 78775-71-0 (1-methyl-cyclohexyl)-malonic acid 
• 57093-55-7 (1-Methylcyclohexyl)cyanessigsaeure-ethylester 
• 1552-92-7 ethyl cyclohexylideneacetate 
• 99062-31-4 (1-methylcyclohexyl)acetonitrile 
• 57093-66-0 (1-Methylcyclohexyl)cyanessigsaeure 
• 78775-64-1 (1-Methylcyclohexyl)malonsaeure-diethylester 
• 108-94-1 cyclohexanone 
• 41589-43-9 cyclohexylidene malonic acid diethyl ester 
• 592478-50-7 (1-methyl-cyclohexyl)-acetic acid ethyl ester 
• 6802-76-2 ethyl 2-cyano-2-cyclohexylideneacetate 
• 931-78-2 1-chloro-1-methylcyclohexane 
• 75-35-4 1,1-Dichloroethylene 
• 590-67-0 1-Methylcyclohexanol 

Downstream Products

• 103038-93-3 (1-methyl-cyclohexyl)-acetic acid amide 
• 82495-11-2 2-(1-methylcyclohexyl)ethanol 
• 666725-82-2 C₂₇H₃₆N₄O₆S 
• 666725-08-2 C₂₇H₃₆N₄O₆S 
• 1318803-59-6 C₁₀H₁₈N₂ 
• 1318803-60-9 C₁₅H₂₇NO₄ 
• 1318803-62-1 C₂₇H₄₄N₄O₆S 
• 698346-11-1 C₂₂H₃₆N₄O₄S 
• 666726-05-2 C₂₇H₃₈N₄O₆S 
• 666725-89-9 C₂₈H₄₁N₅O₅ 
• 666725-78-6 C₂₈H₄₁N₅O₅ 
• 710942-17-9 1-methylcyclohexyl alanine 
• 1588498-68-3 ethyl 2-(4-oxo-3-(2,3,5,6-tetrafluoro-4-(trifluoromethyl)phenyl)-3-azaspiro[5.5]undecan-2-yl)acetate 

Relevant academic research and scientific papers

Distal γ-C(sp3)?H Olefination of Ketone Derivatives and Free Carboxylic Acids

Reported herein is the distal γ-C(sp3)?H olefination of ketone derivatives and free carboxylic acids. Fine tuning of a previously reported imino-acid directing group and using the ligand combination of a mono-N-protected amino acid (MPAA) and an electron-deficient 2-pyridone were critical for the γ-C(sp3)?H olefination of ketone substrates. In addition, MPAAs enabled the γ-C(sp3)?H olefination of free carboxylic acids to form diverse six-membered lactones. Besides alkyl carboxylic acids, benzylic C(sp3)?H bonds also could be functionalized to form 3,4-dihydroisocoumarin structures in a single step from 2-methyl benzoic acid derivatives. The utility of these protocols was demonstrated in large scale reactions and diversification of the γ-C(sp3)?H olefinated products.

Ligand-Enabled γ-C(sp3)?H Olefination of Free Carboxylic Acids

We report the ligand-enabled C?H activation/olefination of free carboxylic acids in the γ-position. Through an intramolecular Michael addition, δ-lactones are obtained as products. Two distinct ligand classes are identified that enable the challenging palladium-catalyzed activation of free carboxylic acids in the γ-position. The developed protocol features a wide range of acid substrates and olefin reaction partners and is shown to be applicable on a preparatively useful scale. Insights into the underlying reaction mechanism obtained through kinetic studies are reported.

Carbon chain shape selectivity by the mouse olfactory receptor OR-I7

The rodent OR-I7 is an olfactory receptor exemplar activated by aliphatic aldehydes such as octanal. Normal alkanals shorter than heptanal bind OR-I7 without activating it and hence function as antagonists in vitro. We report a series of aldehydes designed to probe the structural requirements for aliphatic ligand chains too short to meet the minimum approximate 6.9 ? length requirement for receptor activation. Experiments using recombinant mouse OR-I7 expressed in heterologous cells show that in the context of short aldehyde antagonists, OR-I7 prefers binding aliphatic chains without branches, though a single methyl on carbon-3 is permitted. The receptor can accommodate a surprisingly large number of carbons (e.g. ten in adamantyl) as long as the carbons are part of a conformationally constrained ring system. A rhodopsin-based homology model of mouse OR-I7 docked with the new antagonists suggests that small alkyl branches on the alkyl chain sterically interfere with the hydrophobic residues lining the binding site, but branch carbons can be accommodated when tied back into a compact ring system like the adamantyl and bicyclo[2.2.2]octyl systems.

Intramolecular insertions into unactivated C(sp3)-H bonds by oxidatively generated β-diketone-α-gold carbenes: Synthesis of cyclopentanones

Generation of reactive α-oxo gold carbene intermediates via gold-catalyzed oxidation of alkynes has become an increasing versatile strategy of replacing hazardous diazo carbonyl compounds with benign and readily available alkynes in the development of efficient synthetic methods. However, one of the hallmarks of metal carbene/carbenoid chemistry, i.e., insertion into an unactivated C(sp3)-H bond, has not be realized. This study reveals for the first time that this highly valuable transformation can be readily realized intramolecularly by oxidatively generated β-diketone-α-gold carbenes using ynones as substrates. Substrate conformation control via the Thorpe-Ingold effect is the key design feature that enables generally good to excellent efficiencies, and synthetically versatile cyclopentanones including spiro-, bridged, and fused bicyclic ones can be readily accessed.

Azepanone-based inhibitors of human cathepsin S: Optimization of selectivity via the P2 substituent

A series of azepanone inhibitors of cathepsin S is described. Selectivity over both cathepsin K and cathepsin L was achieved by varying the P2 substituent. Ultimately, a balanced potency and selectivity profile was achieved in compound 39 possessing a 1-methylcyclohexyl alanine at P2 and nicotinamide as the P′ substituent. The cellular potency of selected analogs is also described.

Inhibitors of Serine Proteases

The present invention relates to compounds that inhibit serine protease activity, particularly the activity of hepatitis C virus NS3-NS4A protease. As such, they act by interfering with the life cycle of the hepatitis C virus and are also useful as antiviral agents. The invention further relates to compositions comprising these compounds either for ex vivo use or for administration to a patient suffering from HCV infection. The invention also relates to methods of treating an HCV infection in a patient by administering a composition comprising a compound of this invention.

INHIBITORS OF SERINE PROTEASES FOR THE TREATMENT OF HCV INFECTIONS

The present invention relates to compounds of formula (I): or a pharmaceutically acceptable salt thereof. These compounds inhibit serine protease, particularly the hepatitis C virus NS3-NS4A protease.

INHIBITORS OF SERINE PROTEASES

The present invention relates to compounds of formula (I): or a pharmaceutically acceptable salt or mixtures thereof that inhibit serine protease activity, particularly the activity of hepatitis C virus NS3-NS4A protease.

HEPATITIS C INHIBITOR DIPEPTIDE ANALOGS

The present invention relates to compounds of formula (I): wherein R1, R2, R4, n and m are as defined herein and R3 is selected from: (i) -C(O)OR31 wherein R31 is (C1-6)alkyl or aryl, wherein the (C1-6)alkyl is optionally substituted with one to three halogen substituents; (ii) -C(O)NR32R33, wherein R32 and R33 are each independently selected form H, (C1-6)alkyl, and Het; (iii) -SOvR34, wherein v is 1 or 2 and R34 is selected from: (C1-6)alkyl, aryl, Het, and NR32R33 wherein R32 and R33 are as defined above; and (iv) -CO(O)-R35, wherein R35 is selected from (C1-8)alkyl, (C3-7)cycloalkyl-(C1-4)alkyl, aryl, aryl-(C1-6)alkyl, Het and Het-(C1-6)alkyl, each of which are optionally substituted with one or more substituents each independently selected from halo, (C1-6)alkyl, (C3-7)cycloalkyl, aryl, Het, hydroxyl, -O-(C1-6)alkyl, -S-(C1-6)alkyl, -SO-(C1-6)alkyl, -SO2-(C1-6)alkyl, -O-aryl, -S-aryl, -SO-aryl and -SO2-aryl, wherein the aryl portion of the -O-aryl, -S-aryl, -SO-aryl and -SO2-aryl are each optionally substituted with one to five halo substituents. The present invention further relates to pharmaceutical compositions containing the compounds of formula (I) and methods for using these analogs in the treatment of HCV infection.