72235-51-9

Usage

Chemical Properties

Colorless to light yellow liqui

InChI:InChI=1/C7H7F2N/c8-6-3-1-2-5(4-10)7(6)9/h1-3H,4,10H2/p+1

Upstream product

• 21524-39-0 2,3-difluorobenzonitrile 
• 923845-93-6 2-(3-chloro-2-fluorobenzyl)-4,5-dihydroxyisoindoline-1,3-dione 
• 113211-94-2 2,3-difluorobenzyl bromide 

Downstream Products

• 957112-79-7 C₃₃H₄₀F₃N₃O₆ 
• 480458-49-9 C₂₇H₂₃F₃N₆ 
• 1229011-33-9 (2Z,4Z)-N-(2,3-difluorobenzyl)-8,9-difluoro-5-(2-hydroxyphenyl)-1H-benzo[C]azepine-4-carboxamide 
• 1111266-29-5 C₂₈H₂₉F₂N₉OS 
• 1394930-52-9 2-amino-5-bromo-N-[(2,3-difluorophenyl)methyl]pyridine-3-carboxamide 
• 936219-35-1 3-(2,3-dichlorophenyl)-4-(2,3-difluorobenzyl)-4H-1,2,4-triazole 

Relevant academic research and scientific papers

MUSCARINIC M1 RECEPTOR POSITIVE ALLOSTERIC MODULATORS

The present invention relates to compound of formula (I), or stereoisomers and pharmaceutically acceptable salts as muscarinic M1 receptor positive allosteric modulators. This invention also relates to methods of preparing such compounds and pharmaceutical compositions comprising such compounds. The compounds of this invention are useful in the treatment of various disorders that are related to muscarinic M1 receptor.

HYDRAZIDE, AMIDE, PHTHALIMIDE AND PHTHALHYDRAZIDE ANALOGS AS INHIBITORS OF RETROVIRAL INTEGRASE

The present invention provides catechol-containing hydrazides, amides, phthalimide and phthalhydrazide analogs. These compounds are inhibitors of retroviral integrase, an essential enzyme for the proliferation of retroviruses such as HIV-1. Also provided are pharmaceutical compositions comprising at least one of the catechol-containing hydrazides, amides, phthalimide or phthalhydrazide analogs and a method of using the hydrazide, amide, phthalimide and phthalhydrazide analogs to inhibit retroviral proliferation and as therapeutics for the treatment of AIDS.

The pattern of fluorine substitution affects binding affinity in a small library of fluoroaromatic inhibitors for carbonic anhydrase

(equation presented) A library of fluoroaromatic inhibitors of carbonic anhydrase has been found to bind in a manner dependent on both hydrophobicity and the pattern of substitution of the fluoroaromatic ring. All of the compounds in the library bind to the protein with Kd 3 nM. We have inferred two distinct binding modes from our data, which suggest two types of interactions that should be considered when designing fluorinated drugs.