945414-15-3

Basic information

• Product Name: 7-(o-tolyl)heptanoic acid
• Synonyms: 7-(o-tolyl)heptanoic acid
• CAS NO: 945414-15-3
• Molecular Formula: C₁₄H₂₀O₂
• Molecular Weight: 220.3074
• EINECS: -0
• Mol File: 945414-15-3.mol

Chemical Properties

• Boiling Point: 374.7±21.0 °C(Predicted)
• Appearance: /
• Density: 1.021±0.06 g/cm3(Predicted)
• PKA: 4.77±0.10(Predicted)
• CAS DataBase Reference: 7-(o-tolyl)heptanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 7-(o-tolyl)heptanoic acid(945414-15-3)
• EPA Substance Registry System: 7-(o-tolyl)heptanoic acid(945414-15-3)

Safety Data

• Hazardous Substances Data: 945414-15-3(Hazardous Substances Data)

Upstream product

• 603-35-0 triphenylphosphine 
• 50889-29-7 (5-carboxypentyl)triphenylphosphonium bromide 
• 4224-70-8 6-bromohexanoic acid 

Relevant articles and documents

Synthesis, biological evaluation, and structure activity relationship (SAR) study of pyrrolidine amide derivatives as: N -acylethanolamine acid amidase (NAAA) inhibitors

N-Acylethanolamine acid amidase (NAAA) is one of the key enzymes involved in the degradation of fatty acid ethanolamides (FAEs), especially for palmitoylethanolamide (PEA). Pharmacological blockage of NAAA restores PEA levels, providing therapeutic benefits in the management of inflammation and pain. In the current work, we showed the structure-activity relationship (SAR) studies for pyrrolidine amide derivatives as NAAA inhibitors. A series of aromatic replacements or substituents for the terminal phenyl group of pyrrolidine amides were examined. SAR data showed that small lipophilic 3-phenyl substituents were preferable for optimal potency. The conformationally flexible linkers increased the inhibitory potency of pyrrolidine amide derivatives but reduced their selectivity toward fatty acid amide hydrolase (FAAH). The conformationally restricted linkers did not enhance the inhibitor potency toward NAAA but improved the selectivity over FAAH. Several low micromolar potent NAAA inhibitors were developed, including 4g bearing a rigid 4-phenylcinnamoyl group. Dialysis and kinetic analysis suggested that 4g inhibited NAAA via a competitive and reversible mechanism. Furthermore, 4g showed high anti-inflammatory activities in lipopolysaccharide (LPS) induced acute lung injury (ALI) model, and this effect was blocked by pre-treatment with the PPAR-α antagonist MK886. We anticipate that 4g (E93) will enable a new agent to treat inflammation and related diseases.

TRICYCLIC INHIBITORS OF FATTY ACID AMIDE HYDROLASE

A series of substituted oxazole compounds having an alpha keto side chain at the 2 position and an aromatic, heteroaromatic or heterocycle substituent at the 5 position are disclosed. These compounds exhibit inhibition of fatty acid amid hydrolase and are useful for treatment of malconditions involving that enzyme.

Structure-activity relationships of α-ketooxazole inhibitors of fatty acid amide hydrolase

A systematic study of the structure-activity relationships of 2b (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed targeting the C2 acyl side chain. A series of aryl replacements or substituents for the terminal phenyl group provided effective inhibitors (e.g., 5c, aryl = 1-napthyl, K, - 2.6 nM), with 5hh (aryl -3-ClPh, Ki = 900 pM) being 5-fold more potent than 2b. Conformationally restricted C2 side chains were examined, and many provided exceptionally potent inhibitors, of which 11j (ethylbiphenyl side chain) was established to be a 750 pM inhibitor. A systematic series of heteroatoms (O, NMe, S), electron-withdrawing groups (SO, SO2), and amides positioned within and hydroxyl substitutions on the linking side chain were investigated, which typically led to a loss in potency. The most tolerant positions provided effective inhibitors (12p, 6-position S, Ki = 3 nM, or 13d, 2-position OH, Ki = 8 nM) comparable in potency to 2b. Proteome-wide screening of selected inhibitors from the systematic series of >100 candidates prepared revealed that they are selective for FAAH over all other mammalian serine proteases.