4441-67-2

Upstream product

• 4441-63-8 4-cyclohexylbutanoic acid 
• 79-37-8 oxalyl dichloride 
• 68-12-2 N,N-dimethyl-formamide 
• 1821-12-1 4-Phenylbutyric acid 

Downstream Products

• 102945-33-5 4-cyclohexyl-butyric acid-(1-phenyl-2-pyrrolidino-ethyl ester); hydrochloride 
• 102543-74-8 4-cyclohexyl-butyric acid-(1-phenyl-2-piperidino-ethyl ester); hydrochloride 
• 119211-73-3 3β-(4-cyclohexyl-butyryloxy)-17βH-pregn-5-en-20-yn-17-ol 
• 4441-62-7 4-cyclohexyl-butyric acid amide 
• 18100-05-5 2-(3-cyclohexylpropyl)-3-hydroxy-1,4-naphthoquinone 
• 101255-06-5 4-cyclohexyl-butyric acid anilide 
• 25804-60-8 phenyl 4-cyclohexylbutanoate 
• 91424-56-5 4-Cyclohexyl-N,N-diisobutyl-butyramide 
• 91424-58-7 4-Cyclohexyl-N,N-dihexyl-butyramide 
• 72299-33-3 4-Cyclohexyl-N,N-dipropyl-butyramide 
• 72299-34-4 N,N-Dibutyl-4-cyclohexyl-butyramide 
• 91424-55-4 4-Cyclohexyl-N,N-diisopropyl-butyramide 
• 103230-17-7 γ-Cycloxexylbutyrophenone 
• 180136-25-8 4-cyclohexyl-1-(4-methylphenyl)butan-1-one 

Relevant academic research and scientific papers

Ligand-Assisted Palladium(II)/(IV) Oxidation for sp3C H Fluorination

The direct functionalization of inert sp3C H bonds is limited to a few bond types. Although the activation of sp3C H bonds can be accomplished under mild conditions using palladium catalysts, the subsequent functionalization is not trivial due to the high energy required to convert palladium(II) to palladium(IV). We have systematically studied the palladium oxidation using computation-guided experiments for reactions involving strong chelation control. We find that a mild external ligand could significantly accelerate the oxidation of palladium(II) to palladium(IV) for strong bidentate directing groups. The acceleration is believed to be a result of ligand stabilization of both the palladium(II) and palladium(IV) intermediates. (Figure presented.) .

Pd(II)-catalyzed chelation-assisted cross dehydrogenative coupling between unactivated C(sp3)H bonds in aliphatic amides and benzylic CH bonds in toluene derivatives

The chelation-assisted cross dehydrogenative coupling of C(sp3)H bonds is achieved by the Pd(II)-catalyzed reaction of aliphatic amides that contain a 5-chloro-8-aminoquinoline moiety as the directing group with toluene derivatives in the presence of heptafluoroisopropyl iodide. A variety of functional groups are tolerated.

Trimethylsilyldiazomethane as a versatile stitching agent for the introduction of aziridines into functionalized organic molecules

A highly enantioselective route for the introduction of aziridines into functionalized organic molecules was developed via a tandem acylation and aziridination of TMSCHN2.

Synthesis and SAR of succinamide peptidomimetic inhibitors of cathepsin S

Peptidic, non-covalent inhibitors of lysosomal cysteine protease cathepsin S (1 and 2) were investigated due to low oral bioavailability, leading to an improved series of peptidomimetic inhibitors. Utilizing phenyl succinamides as the P2 residue increased the oral exposure of this lead series of compounds, while retaining selective inhibition of the cathepsin S isoform. Concurrent investigation of the P1 and P2 subsites resulted in the discovery of several potent and selective inhibitors of cathepsin S with good pharmacokinetic properties due to the elimination of saturated aliphatic P2 residues.

α-Aminoalkylphosphonates as a tool in experimental optimisation of P1 side chain shape of potential inhibitors in S1 pocket of leucine- and neutral aminopeptidases

The synthesis and biological activity studies of the series of structurally different α-aminoalkylphosphonates were performed in order to optimise the shape of the side chain of the potential inhibitors in S1 pocket of leucine aminopeptidase [E.C.3.4.11.1]. Analysis of a series of compounds with aromatic, aliphatic and alicyclic P1 side chains enabled to find out the structural features, optimal for that fragment of inhibitors of LAP. The most active among all investigated compounds were the phosphonic analogues of homo-tyrosine (Ki = 120:nM) and homo-phenylalanine (Ki = 140:nM), which even as racemic mixtures were better inhibitors in comparison with the best till now-phosphonic analogue of l-leucine (230 nM). Additional comparison of the inhibitory activity obtained for aminopeptidase N (APN, E.C.3.4.11.2) give insight into structural preferences of both enzymes.

INHIBITORS OF CATHEPSIN S

The present invention provides compounds, compositions and methods for the selective inhibition of cathepsin S. In a preferred aspect, cathepsin S is selectively inhibited in the presence of at least one other cathepsin isozyme. The present invention also provides methods for treating a disease state in a subject by selectively inhibiting cathepsin S.

Chemical process and new intermediates

Process for the preparation of a compound of the general formula (I) and pharmaceutically acceptable salts and solvates thereof, (I) characterised by reacting an N-(amino-tioxo-methyl)-1H-indole-2-carboxamide of the general formula (II), with an α-halogen-ketone of the general formula (III), wherein X stands for halogen.

Non-thiol farnesyltransferase inhibitors: Structure-activity relationships of aralkylsubsituted benzophenones

We describe a novel class of benzophenone-based farnesyltransferase inhibitors exploiting a novel aryl binding region in the farnesyltransferase's active site. The present study was mainly focussed on structural modifications of the trimethylene spacer of the 4-phenyl butyroyl residue of our lead structure (IC50 = 530 nM). These modifications turned out to have little effect on activity as had the replacement of the terminal aryl by cyclohexyl (IC50 = 440 nM vs. IC50 = 530 nM).

Unusual products from dirhodium tetraacetylate-catalyzed decomposition of diazoacetylcycloalkanes

Rh2(OAc)4-assisted decompositions of diazoacetylcycloalkanes are shown to yield cycloalkylacetic acids (Wolff rearrangement), unexpected cycloalkylcarboxylic acids and bicyclic ketones (intramolecular C-H bond insertion). Rh2(OCOF3)4-promoted reactions, on the other hand, have furnished bicyclic ketones and ketene dimers.

New low-density lipoprotein receptor upregulators acting via a novel mechanism

The synthesis and biological activity of a new series of benzamides and related compounds that upregulate the expression of the low-density lipoprotein (LDL) receptor in human hepatocytes (HepG2 cells) by a novel mechanism are described. The lead compound, N-[5-[(3- cyclohexylpropionyl)amino]-2-methylphenyl]-4-hydroxybenzamide (1, RPR102359), increased the expression of the LDL receptors in HepG2 cells by 80% when tested at a concentration of 3 μM. Mevinolin (lovastatin) was found to increase the LDL receptor expression by 70% at the same concentration. In contrast to mevinolin, 1 was found to have no effect on cholesterol biosynthesis in liver homogenates or in HepG2 cells at doses where substantial upregulation of the LDL receptor was observed and thus stimulated LDL receptor expression by a novel mechanism.