919081-42-8

Usage

Uses

Used in Pharmaceutical Industry:
(S)-3-(3-FLUOROPHENYL)-5-(HYDROXYMETHYL)OXAZOLIDIN-2-ONE is used as an impurity in the synthesis of the antibiotic (S)-Tedizolid (T013765) for the treatment of skin-related bacterial infections. Its presence in the synthesis process highlights the need for careful monitoring and control to ensure the purity and efficacy of the final antibiotic product.
Additionally, (S)-3-(3-FLUOROPHENYL)-5-(HYDROXYMETHYL)OXAZOLIDIN-2-ONE can be used as a starting material or intermediate in the development of HIV-1 protease inhibitors with picomolar affinities. These inhibitors are crucial in the fight against HIV/AIDS, as they can effectively block the replication of the virus and help manage the progression of the disease in infected individuals. (S)-3-(3-FLUOROPHENYL)-5-(HYDROXYMETHYL)OXAZOLIDIN-2-ONE's potential in this area underscores its importance in the ongoing research and development of novel antiviral therapies.

InChI:InChI=1/C10H10FNO3/c11-7-2-1-3-8(4-7)12-5-9(6-13)15-10(12)14/h1-4,9,13H,5-6H2/t9-/m0/s1

Upstream product

• 149524-47-0 N-(carbobenzyloxy)-3-fluoroaniline 
• 65031-96-1 (S)-glycidyl butyrate 
• 372-19-0 meta-fluoroaniline 
• 2426-08-6 (R)-3-(Butoxy)-1,2-epoxypropane 

Downstream Products

• 919081-34-8 3-(3-fluoro-phenyl)-2-oxo-oxazolidine-5-carboxylic acid {1-benzyl-2-hydroxy-3-[isobutyl-(4-nitro-benzenesulfonyl)-amino]-propyl}-amide 
• 1066876-00-3 3-(3-fluoro-phenyl)-2-oxo-oxazolidine-5-carbonyl chloride 
• 918543-51-8 (S)-3-(3-fluorophenyl)-2-oxooxazolidine-5-carboxylic acid 

Relevant academic research and scientific papers

Application of spectroscopic methods (FT-IR, Raman, ECD and NMR) in studies of identification and optical purity of radezolid

In the presented study, N-{[(5S)-3-(2-fluoro-4′-{[(1H-1,2,3-triazol-5-ylmethyl)amino]methyl}biphenyl-4-yl)-2-oxo-1,3-oxazolidin-5-yl]methyl}acetamide (radezolid) was synthesized and characterized using FT-IR, Raman, ECD and NMR. The aim of this work was t

An improved efficient synthesis of the antibacterial agent torezolid

An improved and efficient method for the preparation of torezolid based on Suzuki cross-coupling reaction as the key step was developed on a gram scale in five steps. The total yield was 44% and the optical purity of torezolid by the improved method was above 99%.

Structure-based design, synthesis, and structure-activity relationship studies of HIV-1 protease inhibitors incorporating phenyloxazolidinones

A series of new HIV-1 protease inhibitors with the hydroxyethylamine core and different phenyloxazolidinone P2 ligands were designed and synthesized. Variation of phenyl substitutions at the P2 and P2' moieties significantly affected the binding affinity and antiviral potency of the inhibitors. In general, compounds with 2- and 4-substituted phenyloxazolidinones at P2 exhibited lower binding affinities than 3-substituted analogues. Crystal structure analyses of ligand-enzyme complexes revealed different binding modes for 2- and 3-substituted P2 moieties in the protease S2 binding pocket, which may explain their different binding affinities. Several compounds with 3-substituted P2 moieties demonstrated picomolar binding affinity and low nanomolar antiviral potency against patient-derived viruses from HIV-1 clades A, B, and C, and most retained potency against drug-resistant viruses. Further optimization of these compounds using structure-based design may lead to the development of novel protease inhibitors with improved activity against drug-resistant strains of HIV-1.

Discovery of HIV-1 protease inhibitors with picomolar affinities incorporating N-aryl-oxazolidinone-5-carboxamides as novel P2 ligands

Here, we describe the design, synthesis, and biological evaluation of novel HIV-1 protease inhibitors incorporating N-phenyloxazolidinone-5-carboxamides into the (hydroxyethylamino)sulfonamide scaffold as P2 ligands. Series of inhibitors with variations at the P2 phenyloxazolidinone and the P2′ phenylsulfonamide moieties were synthesized. Compounds with the (S)-enantiomer of substituted phenyloxazolidinones at P2 show highly potent inhibitory activities against HIV-1 protease. The inhibitors possessing 3-acetyl, 4-acetyl, and 3-trifluoromethyl groups at the phenyl ring of the oxazolidinone fragment are the most potent in each series, with Ki values in the low picomolar (pM) range. The electron-donating groups 4-methoxy and 1,3-dioxolane are preferred at P2′ phenyl ring, as compounds with other substitutions show lower binding affinities. Attempts to replace the isobutyl group at P1′ with small cyclic moieties caused significant loss of affinities in the resulting compounds. Crystal structure analysis of the two most potent inhibitors in complex with the HIV-1 protease provided valuable information on the interactions between the inhibitor and the protease enzyme. In both inhibitor-enzyme complexes, the carbonyl group of the oxazolidinone ring makes hydrogen-bond interactions with relatively conserved Asp29 residue of the protease. Potent inhibitors from each series incorporating various phenyloxazolidinone based P2 ligands were selected and their activities against a panel of multidrug-resistant (MDR) protease variants were determined. Interestingly, the most potent protease inhibitor starts out with extremely tight affinity for the wild-type enzyme (Ki = 0.8 pM), and even against the MDR variants it retains picomolar to low nanomolar Ki, which is highly comparable with the best FDA-approved protease inhibitors.