23975-61-3

Usage

Uses

Used in Pharmaceutical Industry:
1-(3-CP) is used as a key intermediate in the synthesis of various pharmaceuticals for its ability to contribute to the development of new drugs with improved therapeutic properties. Its reactivity allows for the creation of a diverse range of molecular structures, facilitating the discovery of novel medicinal compounds.
Used in Agrochemical Industry:
In the agrochemical sector, 1-(3-CP) serves as a precursor in the production of agrochemicals, including pesticides and herbicides. Its incorporation into these products can enhance their effectiveness in controlling pests and weeds, thereby improving crop yields and quality.
Used in Fine Chemicals Industry:
1-(3-CP) is utilized as a building block in the preparation of fine chemicals, which are high-purity chemicals used in various applications such as fragrances, dyes, and specialty chemicals. Its versatility in organic synthesis contributes to the creation of a wide array of fine chemicals with specific properties and uses.
Used in Medicinal Chemistry Research:
1-(3-CP) is employed in medicinal chemistry research for its potential biological activities, such as antimicrobial and anti-inflammatory properties. Its study in this field aids in the exploration of new therapeutic agents and the understanding of their mechanisms of action.
Used in Organic Synthesis:
As a diketone compound, 1-(3-CP) is used in organic synthesis for its versatile reactivity, enabling the formation of various chemical structures and compounds. This makes it a valuable component in the development of new materials and chemicals across different industries.

InChI:InChI=1/C10H6ClF3O2/c11-7-3-1-2-6(4-7)8(15)5-9(16)10(12,13)14/h1-4H,5H2

Upstream product

• 383-63-1 ethyl trifluoroacetate, 
• 99-02-5 3'-Chloroacetophenone 

Downstream Products

• 1260243-03-5 ethyl 5-(3-chlorophenyl)-7-(trifluoromethyl)pyrazolo[1,5-a]pyrimidine-3-carboxylate 

Relevant academic research and scientific papers

Pyrazolo[1,5a]pyrimidines as a new class of FUSE binding protein 1 (FUBP1) inhibitors

The transcriptional regulator FUSE binding protein 1 (FUBP1) is aberrantly upregulated in various malignancies, fulfilling its oncogenic role by the deregulation of critical genes involved in cell cycle control and apoptosis regulation. Thus, the pharmaceutical inhibition of this protein would represent an encouraging novel targeted chemotherapy. Here, we demonstrate the identification and initial optimization of a pyrazolo[1,5a]pyrimidine-based FUBP1 inhibitor derived from medium throughput screening, which interferes with the binding of FUBP1 to its single stranded target DNA FUSE. We were able to generate a new class of FUBP1 interfering molecules with in vitro and biological activity. In biophysical assays, we could show that our best inhibitor, compound 6, potently inhibits the binding of FUBP1 to the FUSE sequence with an IC50value of 11.0 μM. Furthermore, hepatocellular carcinoma cells exhibited sensitivity towards the treatment with compound 6, resulting in reduced cell expansion and induction of cell death. Finally, we provide insights into the corresponding SAR landscape, leading to a prospective enhancement in potency and cellular efficacy.

An SAR study of hydroxy-trifluoromethylpyrazolines as inhibitors of Orai1-mediated store operated Ca2+ entry in MDA-MB-231 breast cancer cells using a convenient Fluorescence Imaging Plate Reader assay

The proteins Orai1 and STIM1 control store-operated Ca2+ entry (SOCE) into cells. SOCE is important for migration, invasion and metastasis of MDA-MB-231 human triple negative breast cancer (TNBC) cells and has been proposed as a target for cancer drug discovery. Two hit compounds from a medium throughput screen, displayed encouraging inhibition of SOCE in MDA-MB-231 cells, as measured by a Fluorescence Imaging Plate Reader (FLIPR) Ca2+ assay. Following NMR spectroscopic analysis of these hits and reassignment of their structures as 5-hydroxy-5-trifluoromethylpyrazolines, a series of analogues was prepared via thermal condensation reactions between substituted acylhydrazones and trifluoromethyl 1,3-dicarbonyl arenes. Structure-activity relationship (SAR) studies showed that small lipophilic substituents at the 2- and 3-positions of the RHS and 2-, 3- and 4-postions of the LHS terminal benzene rings improved activity, resulting in a novel class of potent and selective inhibitors of SOCE.

One-pot synthesis of difluoromethyl ketones by a difluorination/fragmentation process

Difluoromethyl ketones are an under-studied class of ketones which have great potential as useful building blocks for materials and drug design. Here we report a simple and convenient synthesis of this class of compounds via a one-pot difluorination/fragm

1,5-Diketones Synthesis via Three-Component Cascade Reaction

A mild and efficient cascade synthesis of 1,5-diketones from readily available N,N-dicyclohexylmethylamine, 1,3-dicarbonyl compounds, and trifluoromethyl β-diketones has been developed. This cascade reaction occurs via an oxidation/Mannich reaction/Cope elimination/Michael addition/retro-Claisen reaction sequence, and provides multiple C-C bond formations in one pot. In addition, exquisite chemoselectivity is achieved in the reaction between 1,3-dicarbonyl compounds and trifluoromethyl β-diketones.

PYRAZOLO AND IMIDAZO-PYRIMIDINE DERIVATIVES

The present invention relates to novel pyrazolo- and imidazo-pyrimidine derivatives of formula (I) wherein A, D, E, L, M, Q, R1, R2 and R3 are as defined in the description and claims and to processes for their preparation, pharmaceutical compositions containing said derivatives and their use in the prevention and treatment of diseases.

Polar substitutions in the benzenesulfonamide ring of celecoxib afford a potent 1,5-diarylpyrazole class of COX-2 inhibitors

Several chemical modifications in the N1-benzenesulfonamide ring of celecoxib are presented. The series with a hydroxymethyl group adjacent to the sulfonamide was found to be the most potent modification that yielded many compounds selectively active against COX-2 enzyme in vitro.