121639-61-0

Basic information

• Product Name: 3,4-DIFLUOROPHENYLACETYL CHLORIDE
• Synonyms: 3,4-DIFLUOROPHENYLACETYL CHLORIDE;2-(3,4-difluorophenyl)acetyl chloride
• CAS NO: 121639-61-0
• Molecular Formula: C₈H₅ClF₂O
• Molecular Weight: 190.57
• Mol File: 121639-61-0.mol
• Article Data: 20

Chemical Properties

• Boiling Point: 224.5±30.0 °C(Predicted)
• Appearance: /
• Density: 1.369±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 3,4-DIFLUOROPHENYLACETYL CHLORIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 3,4-DIFLUOROPHENYLACETYL CHLORIDE(121639-61-0)
• EPA Substance Registry System: 3,4-DIFLUOROPHENYLACETYL CHLORIDE(121639-61-0)

Safety Data

• Hazard Codes: C
• Hazardous Substances Data: 121639-61-0(Hazardous Substances Data)

Upstream product

• 658-93-5 (3,4-difluorophenyl)acetic acid 

Downstream Products

• 1373156-53-6 C₁₄H₉ClF₂O 
• 129409-55-8 ethyl 2-(3,4-difluorophenyl)acetate 
• 1444385-21-0 C₂₅H₂₆F₂N₆O₂ 
• 6831-55-6 2-(3,4-dichlorophenyl)acetyl chloride 
• 935854-71-0 bromo-(3,4-difluoro-phenyl)-acetyl chloride 
• 861393-53-5 2-(3,4-difluorophenyl)acetamide 
• 855316-57-3 2-(R)-(3,4-difluorophenyl)-5-hydroxy-3-(R)-(4-methoxyphenoxymethyl)pentanoic acid N-[(1R,2R)-2-hydroxy-1-methyl-2-phenylethyl]-N-methyl amide 

Relevant articles and documents

Synthesis and biological evaluation of fluorinated N-benzoyl and N-phenylacetoyl derivatives of 3-(4-aminophenyl)-coumarin-7-O-sulfamate as steroid sulfatase inhibitors

In the present work, we report convenient methods for the synthesis of 3-(4-aminophenyl)-coumarin-7-O-sulfamate derivatives N-acylated with fluorinated analogues of benzoic or phenylacetic acid as steroid sulfatase (STS) inhibitors. The design of these potential STS inhibitors was supported by molecular modeling techniques. Additionally, computational docking methods were used to determine the binding modes of the synthesized inhibitors and to identify potential interactions between inhibitors and amino acid residues located in the active site of STS. The inhibitory effects of the synthesized compounds were tested on STS isolated from human placenta and against estrogen receptor-(ER)-positive MCF-7 and T47D cells, as well as ER-negative MDA-MB-231 and SkBr3 cancer cell lines. In the course of our investigation, compounds 6c and 6j demonstrated the highest inhibitory effect in enzymatic STS assays, both with IC50values of 0.18?μM (the IC50value of coumarin-7-O-sulfamate is 1.38?μM, used as a reference). Compound 6j exhibited the highest potency against the MCF-7 and T47D cell lines (15.9?μM and 8.7?μM, respectively). The GI50values of tamoxifen (used as a reference) were 6.8; 10.6; 15.1; 12.5?μM against MCF-7, T47D, MDA-MB-231 and SkBr3 cancer cell lines, respectively. Despite the slightly lower activity of compounds 1 and 2 (both in enzymatic and cell-based experiments) compared to 6g and 6j, analogues 1 and 2 proved to selectively inhibit the growth of ER- and PR-positive cell lines.

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.

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.