434-39-9

Usage

Physical state

Colorless, volatile liquid

Primary use

Solvent in various chemical processes

Additional uses

Production of pharmaceuticals, agrochemicals, and other industrial chemicals

Chemical properties

Strong oxidizing properties

Application

Commonly used as a reagent in organic synthesis

Safety precautions

Handle with caution due to hazardous nature

Potential hazards

Can cause skin and eye irritation upon contact

InChI:InChI=1/C4H6F3NO3/c1-2(8(10)11)3(9)4(5,6)7/h2-3,9H,1H3

Upstream product

• 79-24-3 Nitroethane 
• 421-53-4 2,2,2-trifluoro-1,1-ethanediol 
• 75-90-1 2,2,2-Trifluoroacetaldehyde 
• 433-27-2 ethyl trifluoroacetaldehyde hemiacetal 

Relevant academic research and scientific papers

Inhibition of DD -peptidases by a specific trifluoroketone: Crystal structure of a complex with the actinomadura R39 DD -peptidase

Inhibitors of bacterial dd-peptidases represent potential antibiotics. In the search for alternatives to β-lactams, we have investigated a series of compounds designed to generate transition state analogue structures upon reaction with dd-peptidases. The

Ψ[CH(CF3)NH]Gly-peptides: Synthesis and conformation analysis

Ψ[CH(CF3)NH]Gly peptides, a conceptually new class of peptidomimetics having a stereogenic trifluoroethylamine group as a natural peptide-bond surrogate, have been synthesized by stereoselective addition of α-amino acid esters to trans-3,3,3-tr

Design, synthesis, and evaluation of trifluoromethyl ketones as inhibitors of SARS-CoV 3CL protease

A series of trifluoromethyl ketones as SARS-CoV 3CL protease inhibitors was developed. The inhibitors were synthesized in four steps from commercially available compounds. Three different amino acids were explored in the P1-position and in the P2-P4 positions varying amino acids and long alkyl chain were incorporated. All inhibitors were evaluated in an in vitro assay using purified enzyme and fluorogenic substrate peptide. One of the inhibitors showed a time-dependent inhibition, with a Ki value of 0.3 μM after 4 h incubation.

Peptidomimetic inhibitors of the human cytomegalovirus protease

The development of peptidomimetic inhibitors of the human cytomegalovirus (HCMV) protease showing sub-micromolar potency in an enzymatic assay is described. Selective substitution of the amino acid residues of these inhibitors led to the identification of tripeptide inhibitors showing improvements in inhibitor potency of 27-fold relative to inhibitor 39 based upon the natural tetrapeptide sequence. Small side chains at P1 were well tolerated by this enzyme, a fact consistent with previous observations. The S2 binding pocket of HCMV protease was very permissive, tolerating lipophilic and basic residues. The substitutions tried at P3 indicated that a small increase in inhibitor potency could be realized by the substitution of a tert-leucine residue for valine. Substitutions of the N- terminal capping group did not significantly affect inhibitor potency. Pentafluoroethyl ketones, α,α-difluoro-β-keto amides, phosphonates and α- keto amides were all effective substitutions for the activated carbonyl component and gave inhibitors which were selective for HCMV protease. A slight increase in potency was observed by lengthening the P1' residue of the α-keto amide series of inhibitors. This position also tolerated a variety of groups making this a potential site for future modifications which could modulate the physicochemical properties of these molecules.

Conformation Preferences in Nitro-alcohols: Possible Donor-Acceptor Interactions

By means of 1H and 13C n.m.r. coupling constants, dilution studies, the effect of solvent, and limited i.r. studies, the configuration and conformation in a group of diastereoisomeric nitro-alcohols, such as 3-nitrobutan-2-ol are assigned.The question of interest concerns the effect of intramolecular hydrogen bonding between nitro and hydroxy on conformation.This effect proved to be weak.The OH n.m.r. signal was split into a doublet, in certain cases; the magnitude of the splitting was not indicative of prevalent hydrogen bonding, in agreement with hydroxy chemical shift, and with vicinal proton coupling constants.The 15N chemical shifts were similar to nitromethane, and not sensitive to the state of isomerism.Deuterium for hydrogen exchange occured at the carbon bearing the nitro group with high retention of configuration.