145878-49-5

Basic information

• Product Name: Carbamic acid, [3-[(hydroxyamino)iminomethyl]phenyl]-, 1,1-dimethylethyl ester
• CAS NO: 145878-49-5
• Molecular Formula: C12H17N3O3
• Molecular Weight: 251.285
• Mol File: 145878-49-5.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [3-[(hydroxyamino)iminomethyl]phenyl]-, 1,1-dimethylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [3-[(hydroxyamino)iminomethyl]phenyl]-, 1,1-dimethylethyl ester(145878-49-5)
• EPA Substance Registry System: Carbamic acid, [3-[(hydroxyamino)iminomethyl]phenyl]-, 1,1-dimethylethyl ester(145878-49-5)

Safety Data

• Hazardous Substances Data: 145878-49-5(Hazardous Substances Data)

Upstream product

• 145878-50-8 3-(3-tert-butoxycarbonylamino)benzonitrile 
• 2237-30-1 m-cyanoaniline 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 145899-46-3 [3-(5-oxo-2,5-dihydro-[1,2,4]oxadiazol-3-yl)-phenyl]-carbamic acid tert-butyl ester 
• 886844-76-4 3-(3-aminophenyl)-1,2,4-oxadiazole-5(4H)-thione 

Relevant articles and documents

Design of pentapeptidic BACE1 inhibitors with carboxylic acid bioisosteres at P1′ and P4 positions

We previously reported potent BACE1 inhibitors KMI-420 and KMI-570 possessing a hydroxymethylcarbonyl isostere as a substrate transition-state mimic. Acidic moieties at the P1′ and P4 positions of KMI inhibitors are thought to be unfavorable in terms of membrane permeability across the blood-brain barrier. Herein, we replaced acidic moieties at the P4 position with hydrogen bond accepting groups and acidic moieties at the P1′ position with less acidic and similar molecular-size moieties (carboxylic acid or tetrazole bioisosteres). These inhibitors exhibited improved BACE1 inhibitory activities and a thorough quantitative structure-activity relationship study was performed.

PROCESS FOR THE PREPARATION OF BENZOTRIAZEPINE DERIVATIVES

The present invention is directed to a novel process for the preparation of benzo[e][1,2,4]triazepin-2-one derivatives, useful in the preparation of gastrin and cholecystokinin receptor ligands.

Identification of potent and selective small-molecule inhibitors of caspase-3 through the use of extended tethering and structure-based drug design

The design, synthesis, and in vitro activities of a series of potent and selective small-molecule inhibitors of caspase-3 are described. From extended tethering, a salicylic acid fragment was identified as having binding affinity for the S4 pocket of caspase-3. X-ray crystallography and molecular modeling of the initial tethering hit resulted in the synthesis of 4, which reversibly inhibited caspase-3 with a Ki = 40 nM. Further optimization led to the identification of a series of potent and selective inhibitors with Ki values in the 20-50 nM range. One of the most potent compounds in this series, 66b, inhibited caspase-3 with a Ki = 20 nM and selectivity of 8-500-fold for caspase-3 vs a panel of seven caspases (1, 2, and 4-8). A high-resolution X-ray cocrystal structure of 4 and 66b supports the predicted binding modes of our compounds with caspase-3.