676348-45-1

Usage

Uses

Used in Pharmaceutical Industry:
(2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE is used as a synthetic reagent for introducing the (2-chloro-4-fluorophenyl)acetyl group into organic molecules, which is crucial for the development of new pharmaceuticals. Its unique structure contributes to the creation of novel drug candidates with potential therapeutic properties.
Used in Agrochemical Industry:
In the agrochemical sector, (2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE serves as a key intermediate in the synthesis of various agrochemicals. Its incorporation into these compounds can enhance their effectiveness in pest control and crop protection.
Used in Dye and Perfume Production:
(2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE is utilized in the production of dyes and perfumes due to its ability to impart specific color and fragrance characteristics to these products. Its unique chemical structure allows for the creation of novel dyes with improved properties and perfumes with distinct scents.
Used in Organic Synthesis:
As a versatile building block, (2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE is widely used in organic synthesis for the preparation of fine chemicals. Its reactivity and functional group make it suitable for various chemical reactions, leading to the formation of a diverse range of organic compounds.
Due to its reactive nature, (2-CHLORO-4-FLUORO-PHENYL)-ACETYL CHLORIDE requires careful handling and storage to ensure safety and maintain its integrity for use in various applications.

Upstream product

• 177985-32-9 2-(2-chloro-4-fluorophenyl)acetic acid 

Relevant academic research and scientific papers

Identification of BR102910 as a selective fibroblast activation protein (FAP) inhibitor

Fibroblast activation protein (FAP) belongs to the family of prolyl-specific serine proteases and displays both exopeptidase and endopeptidase activities. FAP expression is undetectable in most normal adult tissues, but is greatly upregulated in sites of tissue remodeling, which include fibrosis, inflammation and cancer. Due to its restricted expression pattern and dual enzymatic activities, FAP inhibition is investigated as a therapeutic option for several diseases. In the present study, we described the structure–activity relationship of several synthesized compounds against DPPIV and prolyl oligopeptidase (PREP). In particular, BR102910 (compound 24) showed nanomolar potency and high selectivity. Moreover, the in vivo FAP inhibition study of BR102910 (compound 24) using C57BL/6J mice demonstrated exceptional profiles and satisfactory FAP inhibition efficacy. Based on excellent in vitro and in vivo profiles, the potential of BR102910 (compound 24) as a lead candidate for the treatment of type 2 diabetes is considered.

Design, synthesis and biological evaluation of novel pyrrolidone-based derivatives as potent p53-MDM2 inhibitors

Inhibition of the interactions of the tumor suppressor protein p53 with its negative regulators MDM2 in vitro and in vivo, representing a valuable therapeutic strategy for cancer treatment. The natural product chalcone exhibited moderate inhibitory activity against MDM2, thus based on the binding mode between chalcone and MDM2, a hit unsaturated pyrrolidone scaffold was obtained through virtual screening. Several unsaturated pyrrolidone derivatives were synthesized and biological evaluated. As a result, because the three critical hydrophobic pockets of MDM2 were occupied by the substituted-phenyl linked at the pyrrolidone fragment, compound 4 h demonstrated good binding affinity with the MDM2. Additionally, compound 4 h also showed excellent antitumor activity and selectivity, and no cytotoxicity against normal cells in vitro. The further antitumor mechanism studies were indicated that compound 4 h could successfully induce the activation of p53 and corresponding downstream p21 proteins, thus successfully causing HCT116 cell cycle arrest in the G1/M phase and apoptosis. Thus, the novel unsaturated pyrrolidone p53-MDM2 inhibitors could be developed as novel antitumor agents.

Phosphonic acid analogs of fluorophenylalanines as inhibitors of human and porcine aminopeptidases N: Validation of the importance of the substitution of the aromatic ring

A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results from the placement of aromatic side chain of an inhibitor. Interestingly, both enantiomers of the individual compounds are usually bound quite similarly.

Synthesis of (2-chlorophenyl)(phenyl)methanones and 2-(2-chlorophenyl)-1- phenylethanones by Friedel-Crafts acylation of 2-chlorobenzoic acids and 2-(2-chlorophenyl)acetic acids using microwave heating

Several 2-(2-chlorophenyl)-1-phenylethanones and (2-chlorophenyl)(phenyl) methanones were prepared by the Friedel-Crafts acylation reaction of 2-(2-chlorophenyl) acetic acids and 2-chlorocarboxylic acids, respectively, in the presence of cyanuric chloride, pyridine, and AlCl3 or FeCl 3 using microwave heating. The yields of the ketones were significantly higher than those obtained using conventional heating. In addition, similar reactions carried out with the less inexpensive and less toxic FeCl3 gave titled ketones in comparable yields. Interestingly, the FeCl3 catalyzed reactions gave pure ketones (no chromatographic purification required), whereas the AlCl3 catalyzed reaction gave impure product that required chromatographic purification.