108716-30-9

Upstream product

• 536-90-3 m-Anisidine 
• 501-53-1 benzyl chloroformate 
• 2398-37-0 3-methoxyphenyl bromide 
• 621-84-1 O-benzyl carbamate 
• 104-57-4 benzyl formate 
• 60144-52-7 tert-butyl 3-methoxyphenylcarbamate 
• 3422-03-5 benzyloxycarbonyl azide 
• 10365-98-7 3-methoxyphenylboronic acid 

Downstream Products

• 18908-07-1 3-methoxyphenyl isocyanate 
• 100-51-6 benzyl alcohol 
• 919081-46-2 (S)-5-(hydroxymethyl)-3-(3-methoxyphenyl)oxazolidin-2-one 
• 1428632-22-7 C₁₅H₁₄FNO₃ 
• 536-90-3 m-Anisidine 
• 918543-56-3 (S)-3-(3-methoxyphenyl)-2-oxooxazolidine-5-carboxylic acid 
• 1066876-05-8 3-(3-methoxy-phenyl)-2-oxo-oxazolidine-5-carbonyl chloride 

Relevant academic research and scientific papers

Synthesis of N-Benzylated Anilines from the Reaction of Anilines and Benzyl Chloroformate

Reactions of benzyl chloroformate with a series of substituted anilines produced N-carbobenzyloxy "CBZ" products along with the unexpected N-benzylated "Bn" compounds. Reaction of aniline, 1a, gave the CBZ, or 2a, and Bn, or 3a, products in 29% and 14% yi

One stone two birds: Cobalt-catalyzed in situ generation of isocyanates and benzyl alcohols for the synthesis of N-aryl carbamates

An efficient method for the synthesis of N-aryl carbamates from N-Boc-protected amines has been developed. The cobalt-catalyzed in situ generation of isocyanates from N-Boc-protected amines and benzyl alcohols from benzyl formates has been achieved for the first time, which in turn furnished the corresponding benzyl carbamates in moderate to high yields. The reaction was catalyzed by CoI2 with tris-(4-dimethylaminophenyl)-phosphine as the ligand and zinc powder as the reductant. The developed reaction conditions were found to be compatible for aromatic amines with both electron-donating and -withdrawing substituents.

N-Arylation of Carbamates through Photosensitized Nickel Catalysis

A highly efficient method of visible light mediated Ni(II)-catalyzed photoredox N-arylation of Cbz-amines/Boc-amines with aryl electrophiles at room temperature is reported. The methodology provides a common access to a wide variety of N-aromatic and N-heteroaromatic carbamate products that find use in the synthesis of several biologically active molecules and provides a distinct advantage over traditional palladium-catalyzed Buchwald reaction.

Synthesis, biological evaluation and mechanism study of a class of cyclic combretastatin A-4 analogues as novel antitumour agents

In the course of our search for novel antitumor agents, a series of cyclic combretastatin A-4 (CA-4) analogues bearing an amide group, A-B or B-C ring condensation, and CC or CN bond in the B ring were designed, synthesized and identified as new microtubule inhibitors. The structure-activity relationship (SAR) studies showed that the hexa-cyclic compounds bearing B-C ring condensation, containing a CC bond in the B ring (4a) provided excellent antiproliferative activities at nanomolar concentrations against various cancer cell lines (IC50 = 46-80 nM). 4a inhibited tubulin assembly at a micromolar range (IC50 = 2.56 ± 0.15 μM) as evidenced by a molecular docking study, which revealed that 4a exerted tubulin polymerisation inhibitory activity by binding to the colchicine binding site of tubulin. Further molecular biology studies showed that 4a disrupted intracellular microtubule polymerisation and thus induced G2/M phase arrest and apoptotsis in A549 cells. Altogether, these results we obtained can guide the design of novel potent molecules for future development.

A synthetic approach to N -aryl carbamates via copper-catalyzed Chan-Lam coupling at room temperature

A mild and efficient synthesis of N-arylcarbamates was achieved by reacting azidoformates with boronic acids in the presence of 10 mol % of copper chloride catalyst. The reaction proceeds readily in an open flask at room temperature without additional base, ligand, or additive. Rapid access to urea analogues via a two-step one-pot procedure is enabled by reacting N-arylcarbamates with aluminum-amine complexes. In addition, among several boronic acid derivatives prepared, dimethylphenyl boronate was found to react rapidly in its reaction with benzyl azidoformate, invoking in situ generation of this species in the catalytic cycle.

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.