21389-46-8

Upstream product

• 626-86-8 adipinic acid monoethyl ester 
• 1071-71-2 ethyl 6-chloro-6-oxohexanoate 
• 4144-62-1 5-benzoylvaleric acid 
• 5581-75-9 6-phenylhexanic acid 

Downstream Products

• 667871-14-9 3-[1-methyl-4-(6-phenyl-hexanoyl)-1H-pyrrol-2-yl]-acrylic acid ethyl ester 
• 667871-36-5 3-[1-methyl-4-(6-phenyl-hexanoyl)-1H-pyrrol-2-yl]-acrylic acid 
• 1071000-99-1 1,1,1,2,2-pentafluoro-8-phenyl-octan-3-one 
• 88343-63-9 2-(6-phenyl-1-oxohexyl)thiophene 
• 22799-74-2 2-hydroxy-3-(5-phenyl-pentyl)-[1,4]naphthoquinone 
• 860-59-3 Di-(ε-phenyl-caproyl)-peroxid 
• 31274-14-3 6-phenylhexanamide 
• 17777-31-0 6-phenylhexanenitrile 
• 1236051-53-8 1-bromo-7-phenylheptan-2-one 
• 1236051-55-0 tert-butyl 2-amino-4-(5-phenylpentyl)-1H-imidazole-1-carboxylate 
• 1622426-52-1 1-(6-phenylhexanoyl)-1H-pyrazole-4-carbonitrile 
• 1622426-51-0 1-(4-methyl-1H-pyrazol-1-yl)-6-phenylhexan-1-one 
• 1622426-50-9 6-phenyl-1-(1H-pyrazol-1-yl)hexan-1-one 
• 1071001-12-1 1,1,1,2,2,3,3-heptafluoro-9-phenylnonan-4-one 

Relevant academic research and scientific papers

N-Acyl pyrazoles: Effective and tunable inhibitors of serine hydrolases

A series of N-acyl pyrazoles was examined as candidate serine hydrolase inhibitors in which the active site acylating reactivity and the leaving group ability of the pyrazole could be tuned not only through the nature of the acyl group (reactivity: amide

N-Acylethanolamine Hydrolyzing Acid Amidase (NAAA) Inhibitors And Use Thereof

Disclosed herein are compounds represented by Structural Formula I: or a pharmaceutically acceptable salt thereof. Values for the variables in Structural Formula I are described herein. The compounds can be used to modulate (e.g., inhibit) N-acylethanolam

3-Phenylalkyl-2H-chromenes and -chromans as novel rhinovirus infection inhibitors

Following our studies on structure-activity relationships of anti-rhinovirus chromene and chroman derivatives, we designed and synthesized new series of 3-phenylalkyl-2H-chromenes and -chromans bearing differently sized, aliphatic linker chains between the two cycles. The cytotoxicity and the antiviral activity of the new compounds on human rhinovirus (HRV) serotype 1B and 14 infection were evaluated in HeLa cell cultures. Most of the tested compounds interfered with HRV1B multiplication in the micromolar or submicromolar concentrations while HRV14 was less susceptible. 3-[3-(4-Chlorophenyl)propyl]chroman (9c) was selected for preliminary mechanism of action studies due to its potent activity against both serotypes (IC50 of 0.48?μM and 1.36?μM towards HRV1B and 14, respectively) coupled with high selectivity (SI?=?206.18 and 73.26, respectively). Results of time of addition/removal studies suggest that 9c, similarly to related derivatives, behaves as a capsid binder interfering with some early events of the HRV1B infectious cycle.

Design, synthesis, and biological evaluation of oxazolidone derivatives as highly potent N-acylethanolamine acid amidase (NAAA) inhibitors

N-Acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme that catalyzes the hydrolysis of endogenous fatty acid ethanolamides (FAEs), such as N-palmitoylethanolamide (PEA). PEA exhibits anti-inflammatory and analgesic activities by engaging peroxisome proliferator-activated receptor α (PPAR-α). Preventing PEA degradation by inhibition of NAAA has been proposed as a novel strategy for the treatment of inflammation and pain. In the present study, we reported the discovery of the oxazolidone derivative as a novel scaffold for NAAA inhibitors, and studied the structure-activity relationship (SAR) by modification of the side chain and terminal lipophilic substituents. The results showed that the link chain length of C5, straight and saturated linkages were the preferred shape patterns for NAAA inhibition. Several nanomolar NAAA inhibitors were described, including 2f, 3h, 3i and 3j with IC50 values of 270 nM, 150 nM, 100 nM and 190 nM, respectively. Enzymatic degradation studies suggested that 2f inhibited NAAA in a selective, noncompetitive and reversible pattern. Moreover, 2f showed high anti-inflammatory and analgesic activities after systemic and oral administration.

Inhibition of bacterial biofilms and microbial growth with imidazole derivatives

Disclosure is provided for imidazole derivative compounds useful to inhibit the formation of biofilms and/or inhibit microbial growth, compositions including these compounds, devices including these compounds, and methods of using the same.

Benzoxazolone carboxamides: Potent and systemically active inhibitors of intracellular acid ceramidase

The ceramides are a family of bioactive lipid-derived messengers involved in the control of cellular senescence, inflammation, and apoptosis. Ceramide hydrolysis by acid ceramidase (AC) stops the biological activity of these substances and influences surv

Discovery libraries targeting the major enzyme classes: The serine hydrolases

Two libraries of modestly reactive ureas containing either electron-deficient acyl anilines or acyl pyrazoles were prepared and are reported as screening libraries for candidate serine hydrolase inhibitors. Within each library is a small but powerful subs

RCAI-84, 91, and 105-108, ureido and thioureido analogs of KRN7000: Their synthesis and bioactivity for mouse lymphocytes to produce Th1-biased cytokines

RCAI-84, 91, and 105-108 (1-6), the analogs of KRN7000 (A) with a ureido or a thioureido linkage instead of a carboxamido bond, were synthesized to examine their immunostimulatory activity against mouse lymphocytes. According to their bioassay, the ureido

Hypervalent iodine catalyzed hofmann rearrangement of carboxamides using oxone as terminal oxidant

Hofmann rearrangement of carboxamides to carbamates using Oxone as an oxidant can be efficiently catalyzed by iodobenzene. This reaction involves hypervalent iodine species generated in situ from catalytic amount of PhI and Oxone in the presence of 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) in aqueous methanol solutions. Under these conditions, Hofmann rearrangement of various carboxamides affords corresponding carbamates in high yields.

Potent and selective fluoroketone inhibitors of group VIA calcium-independent phospholipase A2

Group VIA calcium-independent phospholipase A2 (GVIA iPLA 2) has recently emerged as a novel pharmaceutical target. We have now explored the Structure-activity relationship between fluoroketones and GVIA iPLA2 inhibition. The presence of a naphthyl group proved to be of paramount importance. 1,1,1-Trifluoro-6-(naphthalen-2-yl)hexan-2-one (FKGK18) is the most potent inhibitor of GVIA iPLA2 (XI(50) = 0.0002) ever reported. Being 195 and >455 times more potent for GVIA iPLA 2 than for GIVA cPLA2 and GV sPLA2, respectively, makes it a valuable tool to explore the role of GVIA iPLA 2 in cells and in vivo models. 1,1,1,2,2,3,3-Heptafluoro-8- (naphthalene-2-yl)octan-4-one inhibited GVIA iPLA2 with a X I(50) value of 0.001 while inhibiting the other intracellular GIVA cPLA2 and GV sPLA2 at least 90 times less potently. Hexa- and octafluoro ketones were also found to be potent inhibitors of GVIA iPLA 2; however, they are not selective.