21239-29-2

Usage

Uses

Ethyl 3,5-Dimethylbenzoate can be used as olefin polymerization catalyst.

InChI:InChI=1/C11H14O2/c1-4-13-11(12)10-6-8(2)5-9(3)7-10/h5-7H,4H2,1-3H3

Upstream product

• 556-96-7 5-bromo-1,3-xylene 
• 1906-57-6 potassium monoethyl oxalate 
• 780-69-8 triethoxyphenylsilane 
• 6613-44-1 3,5-dimethylbenzoyl chloride 
• 64-17-5 ethanol 
• 25081-39-4 methyl 3,5-dimethylbenzoate 
• 108-67-8 1,3,5-trimethyl-benzene 
• 499-06-9 3,5-dimethylbenzoic acid 

Downstream Products

• 27389-49-7 3,5-dimethylbenzohydrazide 
• 503818-85-7 5-(3,5-dimethyl-phenyl)-2H-pyrazol-3-ylamine 
• 220286-07-7 3-Bromomethyl-5-methylbenzoic acid, ethyl ester 
• 765312-46-7 2-(3',5'-dimethylphenyl)-1-pyrroline 
• 1386874-29-8 ethyl 3,5-diformylbenzoate 
• 383127-44-4 2-(3,5-dimethylphenyl)pyrrolidine 

Relevant academic research and scientific papers

Design, synthesis and biological evaluation of N-hydroxy-aminobenzyloxyarylamide analogues as novel selective κ opioid receptor antagonists

Aminobenzyloxyarylamide derivatives 1a-i and 2a-t were designed and synthesized as novel selective κ opioid receptor (KOR) antagonists. The benzoyl amide moiety of LY2456302 was changed into N-hydroxybenzamide and benzisoxazole-3(2H)-one to investigate whether it could increase the binding affinity or selectivity for KOR. All target compounds were evaluated in radioligand binding assays for opioid receptor binding affinity. These efforts led to the identification of compound 1c (κ Ki = 179.9 nM), which exhibited high affinity for KOR. Moreover, the selectivity of KOR over MOR and DOR increased nearly 2-fold and 7-fold, respectively, compared with (±)LY2456302.

Facile, highly efficient and environmentally friendly transesterification mediated by platinum dioxide and nickel oxide under essentially neutral conditions

A practical, facile and highly efficient transesterification reaction under essentially neutral conditions was achieved using platinum dioxide (PtO2) or PtO2/nickel oxide (NiO) as the catalyst. A number of esters and alcohols that contain various functional groups were employed. Good to excellent yields were obtained for different aromatic or aliphatic starting materials. The Pt-alcohol intermediate generated in situ facilitated the exchange of low-alcohol esters to high-alcohol esters.

Design, synthesis and biological evaluation of aminobenzyloxyarylamide derivatives as selective κ opioid receptor antagonists

Opioid receptors play an important role in both behavioral and mood functions. Based on the structural modification of LY2456302, a series of aminobenzyloxyarylamide derivatives were designed and synthesized as κ opioid receptor antagonists. The κ opioid receptor binding ability of these compounds were evaluated with opioid receptors binding assays. Compounds 1a-d showed high affinity for κ opioid receptor. Especially for compound 1c, exhibited a significant Kivalue of 15.7?nM for κ opioid receptor binding and a higher selectivity over μ and δ opioid receptors compared to (±)LY2456302. In addition, compound 1c also showed potent κ antagonist activity with κ IC50?=?9.32?nM in [35S]GTP-γ-S functional assay. The potential use of the representative compounds as antidepressants was also investigated. The most potent compound 1c not only exhibited potent antidepressant activity in the mice forced swimming test, but also displayed the effect of anti-anxiety in the elevated plus-maze test.

Design and optimization of N-acylhydrazone pyrimidine derivatives as E. coli PDHc E1 inhibitors: Structure-activity relationship analysis, biological evaluation and molecular docking study

By targeting the thiamin diphosphate (ThDP) binding site of Escherichia coli (E. coli) pyruvate dehydrogenase multienzyme complex E1 (PDHc E1), a series of novel ‘open-chain’ classes of ThDP analogs A, B, and C with N-acylhydrazone moieties was designed and synthesized to explore their activities against E. coli PHDc E1 in vitro and their inhibitory activity against microbial diseases were further evaluated in vivo. As a result, A1–23 exhibited moderate to potent inhibitory activities against E. coli PDHc E1 (IC50 = 0.15–23.55 μM). The potent inhibitors A13, A14, A15, C2, had strong inhibitory activities with IC50 values of 0.60, 0.15, 0.39 and 0.34 μM against E. coli PDHc E1 and with good enzyme-selective inhibition between microorganisms and mammals. Especially, the most powerful inhibitor A14 could 99.37% control Xanthimonas oryzae pv. Oryzae. Furthermore, the binding features of compound A14 within E. coli PDHc E1 were investigated to provide useful insights for the further construction of new inhibitor by molecular docking, site-directed mutagenesis, and enzymatic assays. The results indicated that A14 had most powerful inhibition against E. coli PDHc E1 due to the establishment of stronger interaction with Glu571, Met194, Glu522, Leu264 and Phe602 at active site of E.coli PDHc E1. It could be used as a lead compound for further optimization, and may have potential as a new microbicide.

Palladium-catalyzed coupling of benzoyl halides with aryltrifluorosilanes leading to diaryl ketones

Acyl-aryl Hiyama coupling of acyl halides with arylsilanes has been achieved by employing a palladium/phosphine catalyst system. A variety of acyl chlorides and fluorides can be applied for coupling with arylsilicon reagents, and unsymmetrical benzophenone derivatives can be prepared using this protocol.

Discovery of novel small molecule inhibitors of dengue viral NS2B-NS3 protease using virtual screening and scaffold hopping

By virtual screening, compound 1 was found to be active against NS2B-NS3 protease (IC50 = 13.12 ± 1.03 μM). Fourteen derivatives (22) of compound 1 were synthesized, leading to the discovery of four new inhibitors with biological activity. In order to expand the chemical diversity of the inhibitors, small-molecule-based scaffold hopping was performed on the basis of the common scaffold of compounds 1 and 22. Twenty-one new compounds (23, 24) containing quinoline (new scaffold) were designed and synthesized. Protease inhibition assays revealed that 12 compounds with the new scaffold are inhibitors of NS2B-NS3 protease. Taken together, 17 new compounds were discovered as NS2B-NS3 protease inhibitors with IC50 values of 7.46 ± 1.15 to 48.59 ± 3.46 μM, and 8 compounds belonging to two different scaffolds are active to some extent against DENV based on luciferase reporter replicon-based assays. These novel chemical entities could serve as lead structures for discovering therapies against DENV.

Diacylhydrazine derivatives as novel potential chitin biosynthesis inhibitors: Design, synthesis, and structure-activity relationship

A series of diacylhydrazine derivatives containing hydrophobic alkyl chains have been designed and synthesized. The target molecules have been identified on the basis of analytical spectral (IR, 1H NMR, 13C NMR, and HRMS) data. All synthesized compounds have been screened for their potential inhibition in vitro against chitin synthesis using yeast cell extracts. The preliminary assays indicate that some of the compounds display moderate to good inhibitory activity. Structure-activity relationship (SAR) is also discussed based on the experimental data, and the further analysis of the quantitative structure-activity relationship (QSAR) indicates that the electronic parameter is the main factor to affect inhibition activities.

Novel 4H-1,3,4-oxadiazin-5(6H)-ones with hydrophobic and long alkyl chains: Design, synthesis, and bioactive diversity on inhibition of monoamine oxidase, chitin biosynthesis and tumor cell

A new series of nitrogen-containing heterocycles 4H-1,3,4-oxadiazin-5(6H)-ones derivatives with hydrophobic and long chains were designed and synthesized by direct cyclization reaction of N′-alkylation substituted aroylhydrazines with chloroacetyl chloride. The preliminary assays showed that some of the compounds displayed moderate to good inhibitory activities toward monoamine oxidase (MAO) at the concentration of 10-5-10-3 M, and antitumor activities against human lung cancer A-549 and human prostate cancer PC-3 cell lines at μM level, which might provide new scaffold for anticancer agents. Furthermore, compounds 5i and 5m exhibited significant inhibitory activity on chitin biosynthesis, which might represent a novel class of highly potential inhibitors of chitin synthesis. Crown Copyright

1,3,4-Oxadiazoline derivatives as novel potential inhibitors targeting chitin biosynthesis: Design, synthesis and biological evaluation

Two series of 1,3,4-oxadiazoline heterocycle derivatives were designed, synthesized and identified. Bioactivity assays showed that all synthesized compounds inhibited chitin synthesis in yeast, suggesting they might be a novel class of potential inhibitors against chitin biosynthesis. The structure-activity relationships (SAR) of these compounds are discussed.