302912-39-6

Usage

Uses

Used in Scientific Research:
3,5-DIFLUOROPHENYL ISOTHIOCYANATE 97 is used as a research chemical for various scientific applications, particularly in the study of isothiocyanates and their reactions.
Used in Pharmaceutical Manufacturing:
3,5-DIFLUOROPHENYL ISOTHIOCYANATE 97 is used as an intermediate or building block in the synthesis of various pharmaceuticals, taking advantage of its unique reactivity and properties.
Used in Chemical Synthesis:
3,5-DIFLUOROPHENYL ISOTHIOCYANATE 97 is used as a reagent in the synthesis of other organic compounds, leveraging its fluorine atoms for specific chemical reactions.
Safety Measures:
Due to its potential hazards, such as causing eye irritation or skin inflammation, 3,5-DIFLUOROPHENYL ISOTHIOCYANATE 97 requires proper handling and safety measures. It is typically stored in a cool, dry place away from heat and flame to prevent any adverse reactions or accidents.

InChI:InChI=1/C7H3F2NS/c8-5-1-6(9)3-7(2-5)10-4-11/h1-3H

Upstream product

• 75-15-0 carbon disulfide 
• 372-39-4 3,5-difluoroaniline 
• 463-71-8 thiophosgene 

Downstream Products

• 1070801-89-6 (Z)-1-(4-bromophenyl)-5-{[(3,5-difluorophenyl)amino](mercapto)methylidene}pyrimidine-2,4,6(1H,3H,5H)-trione 
• 1033590-94-1 C₁₄H₁₂F₂N₂OS 
• 1052260-04-4 1-(3,5-difluorophenyl)-3-(3-oxo-1,3-dihydroisobenzofuran-5-yl)thiourea 
• 838867-31-5 N-(3,5-difluorophenyl)morpholine-4-carbothioamide 
• 1338073-02-1 C₂₂H₁₅F₂N₇S 
• 1338818-39-5 5'-(3,5-difluorophenylamino)-3'H-spiro(indoline-3,2'-[1,3,4]thiadiazole)-2-one 
• 1038978-61-8 4-(3,5-difluoro-phenyl)thiosemicarbazide 
• 1323135-38-1 1-(3,5-difluorophenyl)-3-((1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl)thiourea 
• 1152595-61-3 2-({[2-({[(3,5-difluorophenyl)amino]carbonothioyl}oxy)ethyl]amino}carbonyl)benzoic acid 
• 1152594-71-2 O-[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl] 3,5-difluorophenylthiocarbamate 
• 1043391-78-1 2-[2-({({[2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethoxy][(3,5-difluorophenyl)imino]methyl}dithio)[(3,5-difluorophenyl)imino]methyl}oxy)ethyl]-1,3-dioxoisoindoline 
• 955952-95-1 2-cyano-2-(3,5-difluoro-phenylthiocarbamoyl)-acetamide 

Relevant academic research and scientific papers

Discovery of dual inhibitors targeting both HIV-1 capsid and human cyclophilin A to inhibit the assembly and uncoating of the viral capsid

HIV-1 assembly and disassembly (uncoating) processes are critical for the HIV-1 replication. HIV-1 capsid (CA) and human cyclophilin A (CypA) play essential roles in these processes. We designed and synthesized a series of thiourea compounds as HIV-1 assembly and disassembly dual inhibitors targeting both HIV-1 CA protein and human CypA. The SIV-induced syncytium antiviral evaluation indicated that all of the inhibitors displayed antiviral activities in SIV-infected CEM cells at the concentration of 0.6-15.8 μM for 50% of maximum effective rate. Their abilities to bind CA and CypA were determined by ultraviolet spectroscopic analysis, fluorescence binding affinity and PPIase inhibition assay. Assembly studies in vitro demonstrated that the compounds could potently disrupt CA assembly with a dose-dependent manner. All of these molecules could bind CypA with binding affinities (Kd values) of 51.0-512.8 μM. Fifteen of the CypA binding compounds showed potent PPIase inhibitory activities (IC50 values 1 μM) while they could not bind either to HIV-1 Protease or to HIV-1 Integrase in the enzyme assays. These results suggested that 15 compounds could block HIV-1 replication by inhibiting the PPIase activity of CypA to interfere with capsid disassembly and disrupting CA assembly.

Isothiazoles as active-site inhibitors of HCV NS5B polymerase

Isothiazole analogs were discovered as a novel class of active-site inhibitors of HCV NS5B polymerase. The best compound has an IC50 of 200 nM and EC50 of 100 nM, which is a significant improvement over the starting inhibitor (1). The X-ray complex structure of 1 with HCV NS5B was obtained at a resolution of 2.2 A, revealing that the inhibitor is covalently linked with Cys 366 of the 'primer-grip'. Furthermore, it makes considerable contacts with the C-terminus, β-loop, and more importantly, to the active-site of the enzyme. The uniqueness of this binding mode offers a new insight for the rational design of novel inhibitors for HCV NS5B polymerase.